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Proteomics/Post-translational Modification/Proteolytic Processing

Chapter Edited and Updated by: Vrunda Sheth & Priyanka Yadlapati E-mail: vns4483@rit.edu, pxy8519@rit.edu

This Section:

Introduction
Proteolytic processing is a major form of post translational modification which occurs when a protease cleaves one or more bonds in a target protein to modify its activity. This processing may lead to activation, inhibition or destruction of the protein's activity. Many cellular processes are triggered by proteolytic processing. The attacking protease may remove a peptide segment from either end of the target protein, but it may also cleave internal bonds in the protein that lead to major changes in the structure and function of the protein.

Proprotein

Many proteins are synthesized as inactive precursors, which may be called proproteins or, in the case of enzymes, zymogens. These proproteins are synthesized in one tissue or organ, transported to another tissue or organ and activated there by proteolytic processing.

This figure shows an example of proteolytic cleavage which results in the activation of BID in the process of apoptosis, programmed cell death. BID is a pro-apoptotic protein which contains the BH3 domain, which is also known as the death domain. Capsase-8 is a protease that cleaves BID in the presence of an apoptotic signal to continue the process of apoptosis.

Proteolytic processing is a highly specific process. The mechanism of proteolytic processing varies according to the protein being processed, location of the protein, and protease. There is no general rule of the thumb for proteolytic processing. This section therefore provides different examples of proteolytic processing.

Proteolytic processing in secretory pathways
Proteolysis of precursor proteins regulates many cellular processes including gene expression, embryogenesis, the cell cycle, programmed cell death, intracellular protein targeting and endocrine/neural functions. In all of these processes, proteolytic cleavage of precursor proteins are necessary. The proteolysis is often done by serine proteases in the secretory pathways. These proteases are calcium dependent serine endoproteases and are related to yeast and subtilisin proteases and therefore called Subtilisin-like Proprotein Convertases (SPCs) or PCs. Seven members of this family have been identified & characterized and each have conserved signal peptides, pro-regions, catalytic and P-domains but differ in their C-terminal domains in mammals.

Autocatalytic cleavage of an N-terminal propeptide activates these proteases, which is required for folding and activity also release of  prodomain. It is known from previous studies that folding of the P domain forms an eight-stranded beta barrel to interact through a hydrophobic patch to a catalytic domain. Folding and activity needs a downstream domain of 150 amino acids. Concerning PCs their C-terminal regions play quite a role in subcellular routing. Furin, one of the seven members of the SPCs, serves as a model for other PCs. The intramolecular cleavage of prodomain allows furin to exit the endoplasmic reticulum (ER). Until the cleaved inactive proenzyme reaches the trans Golgi Network (TGN) where dissociation of prodomain is facilitated by calcium-enriched environment and acidic pH conditions, the prodomain remains attached noncovalently to it. For complete activation, further inhibitory reactions take place within the prodomain by a second cleavage. Proinsulin, Proglucagon and Proopiomelanocortin (POMC) are the well studied peptide hormone precursors.

PCs are responsible for the cleavage at specific sites in each of these precursors. The most frequent sites for cleavage are KR and RR. Proglucagon is processed by PC2 in the alpha cells and by PC1/PC3 in the intestinal L cells and releases active forms of glucagons-like peptides namely GLP-1 and GLP-2. The convertases PC2 and PC1/PC3 are majorly expressed in brain and neuroendocrine system to act on neuropeptide precursors in the Secretory pathway. Glucose, the second messengers in the neuroendocrine cells regulates the transcription and translation of PC2 and PC1/PC3. Other convertases like PC4 expressed in testis and an isoform of PC6 that lacks a TM domain belong to PC family. Recently discovered convertases are PC7, Furin, PACE4 and PC6B. These are expressed in tissues like liver, gut, brain, neuroendocrine system. There are still many unidentified enzymes that participate in cleavages at single basic residues and unusual sites, other than the subtilisin-like Proprotein Convertases.

Examples of proteolytic processing in various organs of our body
In concern with the proteolytic processing with respect to kidney the human prorenin is considered. The proteolytic processing of human prorenin in renal tissues is discussed here. The mouse proprotein convertase also known as PC1 accurately cleaves the prorenin and generates active renin. The human Proprotein Convertase also known as PC3 can also process the prorenin to generate renin but not as efficiently as mPC1 does. This is because of the differences in the sequences of the carboxy terminus from PC1 to hybrid hPC1/mPC1. The cleavage of prorenin bay PC1 in humans takes place at a pair of basic amino acids by removal of 43 amino acid prosegment from the amino terminus of the it along with identification of a functionally important site in the hPC1. Also PC1 generates active renin in other tissues like adrenal medulla and certain adrenal tumors. If human prorenin has either in Lys or Arg residues at the cleavage site then the hPC1 cannot generate active rennin.
 * Renal proteins

 * Blood protein

The Kell Blood Group Protein belongs to family of metalloendopeptidases. It’s a membrane Glycoprotein which shares a pentametric zinc-binding consensus sequence. It conserves all the amino acids required for the endopeptidase activity.Kell Blood Group proteins have a homology with M13 family in which a disulphide bond is covalently linked to a protein named XK, this spans the membrane 10 times, whereas kell proteins is linked to XK present is fifth extracellular loop. Activation of endothelins and processing of bioactive peptides can be done by Kell proteins.

Fodrin, Human Brain Alpha Spectrin plays an important role in the nervous system yet its mechanism is not completely understood. Its isoforms are present within the cells and in some neurotransmitter neurons. It is proteolytically processed by the calcium dependent proteases. This processing of fodrin is a central molecular mechanism in the development of long term memory. Foldrin has a proteolytically hypersensitive site in its centre for cleavage. Calcium-dependent binding of calmodulin takes place at this site.
 * Human Brain Spectrin

Autoprocessing
This is the process in which a protein modifies itself to convert a proprotein into an active protein. A classic example of this is the autoprocessing of furin family of endoproteases. Furin is the most widely used proteolytic processing enzyme and functions mainly for cleavage of proproteins needed to maintain cellular physiology.Furin family of protease is also called the PACE family.There are 7 identified members in this family and among them Furin is the most important protein.Most of these PACE family are active in the trans golgi network. Furin is transmembrane protein which is synthesized as a 100KDa protein. This protein undergoes catalytic cleavage in the Endoplasmic reticulum to become active furin which is 94 KDa. The proprotein however remains bound to the protein and acts as the furin inhibitor. The polypeptide release then occurs in the trans golgi network where furin becomes active.

An example of proteolytic processing by furin is processing of ProFibrillin.Fibrillin-1 is a glycoprotein which is a major component of the Extracellular matrix. It undergoes proteolytic cleavage in its C-terminal domain to form fibrillin-1 in the trans golgi network.

Proteolytic processing of the Human Immunodeficiency Virus type 1
Polyprotein precursors are processed to form the proteins that produce the retroviral particle. One of these precursors is the viral protease that processes the precursors itself. This viral protease cleaves the retroviral precursor proteins during the virus assembly. Fully infectious viral particles are produced by precise protease-mediated precursor processing and if the order of the cleavage changes, it results in the less infectious viral particle. To become active the proteases must form a dimer. The processing events are first carried out by the embedded PR, prior to the release from the GagPol precursor.The activated protease domain on one pair of GagPol molecules cleaves initial sites on those same molecules. Further substitutions at the first amino acid in the proteases, a proline, lifts this constraint and free the protease domain within GagPol to cleave additional native processing sites in the precursor not cleaved by the wild-type embedded protease.

Proteolytic processing- role in therapeutics
The fact that certain proteins can modify others by binding to specific site and alter its activity is used as a principle in the development of certain modern therapeutics. Here is an example of how the process of proteolytic processing has been used to find possible cure for diseases. Human coronavirus is the causative agent of the common respiratory disease in adults and children. There are no current cure for CoV as a result proteolytic processing is being exploited to find new drug targets. Biochemical analysis of HCoV –NL63 virus showed 2 viral papain like protease PLP1 and PLP2 which process viral replicase polyprotein. In this case they generated polyclonal antisera against 2 of replicase non structural proteins nsp3 and nsp4. It was found that PLP1 processes clevage site to release 1 to release nsp1 whereas PLP2 released nsp2 and nsp3. Also by using hexa ubiquitin substrate and ubiquitin vinylsulphonate inhibitor specific to deubiquitinization enzyme further show that CoV has deubiquititination activity. Understanding the concept of proteolytic processing and deubiquitinating of PLP’s can pave a way to the development of novel antisera regents directed against HCoV.

Lethal effects of proteolytic processing
Proteolytic processing not only helps in carrying out normal cellular processes but it also can cause processing of proteins to give lethal proteins. A classic example of proteolytic processing which develops lethal protein is development of Netherton syndrome. Netherton syndrome is a autosomal recessive congenital syndrome which causes ichthyosiform erythroderma caused by a mutation in the human SPINK5. Biochemical analysis of Netherton syndrome have shown an increase in the proteolytic processing of profilggrin into its constituent filaggrin monomers. Defects in filagrin processing cause congenital disorders like icthyosis. SPINX5 undergoes extreme proteolytic processing furin is assumed to be involved in the proteolytic processing of SPINX5 however the exact extent of processing is yet to be deteremined. In the absence of serine protease inhibitor SPHINX5 there is abnormal increase in the processing of profilagrin resulting in the increased production of filagrin monomers causing severely compromised epidermail barrier function.


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Proteomics/Protein Primary Structure/Genetic Code

This Section:

Transcription
Transcription is the process by which messenger RNA (mRNA), is synthesized from information encoded by DNA. This is the first step in gene expression and also an important location of cellular control. By careful regulation, a cell is able to change the expression of DNA to RNA which in turn influences the proteome - increasing levels of expression to increase protein products and decreasing expression to limit products. Transcription proceeds by reading from the 3’ → 5’ end of the DNA source (template strand), adding nucleotides to the growing mRNA strand in the 5’ → 3’ direction. These nucleotides are slightly different in RNA compared to DNA. With RNA, uracil (U) is substituted for thymine (T). The resulting RNA strand will have the same sequence (substituting U for T) as the DNA coding strand and a complementary sequence to the DNA template strand.

Transcription can be divided into three processes: initiation, elongation, and termination.

Initiation

In bacteria initiation occurs in the cytoplasm when RNA polymerase binds to the DNA at a promoter site, shown in the attached image, and then the associated helicase begins to separate the DNA double helix. Along with RNA polymerase comes a variety of additional molecules that together form the machinery needed to transcribe a gene.

The initiation process in eukaryotes occurs in the nucleus and is more complex due to finer levels of regulation. For starters, there are a battery of different RNA polymerase enzymes present in eukaryotes, of which RNA polymerase II is the one responsible for the transcription of mRNA. There is not a simple promoter sequence for RNA polymerase to bind as there is in bacteria, but a combination of a promoter sequences and various transcription factors is required for binding of RNA polymerase. There are also repressors, which are proteins that bind DNA near a promoter and prevent initiation of transcription. A gene product itself may in fact be a repressor, exhibiting feedback inhibition, where as the concentration of the product builds, further production is slowed.

Elongation

Elongation is the process by which RNA polymerase adds complementary bases to the growing mRNA strand in the 5' → 3' (reading the template strand from 3' → 5'), one at a time until reaching a termination point. The energy for this process is provided by the hydrolysis of the nucleoside triphosphates (NTPs) that are the building blocks for mRNA. For each base added to the growing mRNA chain, one NTP is converted to the corresponding NMP plus inorganic pyrophosphate. As RNA polymerase travels down the template strand, helicase travels ahead of it "unzipping" the DNA double helix as it goes, shown in the image to the right.

During elongation, RNA polymerase alternately works at full speed for approximately 100 bases and then stops. This pattern of starts and stops has led scientists to determine that there are proofreading mechanisms being employed by RNA polymerase. There is also evidence of RNA polymerase "backtracking", or going back over bases that are already paired, again assumed to be part of a proofreading mechanism. In bacteria, there are two such known proofreading mechanisms, pyrophosphorolytic editing is where the incorrect base pair is immediately removed and hydrolytic editing is where RNA polymerase has to backtrack to fix an incorrect pairing. Less is known about eukaryotic proofreading methods.

Termination

Termination is the end of transcription, when an mRNA strand is fully formed. As seen in the image to the right, both the newly formed mRNA and the RNA polymerase complex dissociate from the DNA template. Termination in prokaryotes can follow one of two forms, Rho-independent (intrinsic termination) and Rho-dependent. Rho is protein factor that, in a Rho-dependent termination, functions to bind RNA and hydrolyze ATP, destabilizing the link between the template strand and the newly formed mRNA and releasing the mRNA. In a Rho-independent termination, there is a termination sequence on the template strand, causing RNA polymerase to cease its activity and fall off the template.

In eukaryotes, termination is more complex and not as well understood. Some eukaryotic transcription proceeds well past the termination point and the additional nucleotides are later removed from the transcript, some transcription is mediated by termination factors and some methods of termination are still uncharacterized. After termination in eukaryotes, it is very common for the mRNA to undergo Post Transcriptional Modifications. These include the addition of a 5' cap to ensure the mRNA stability. Addition of a Poly-A tail is also an important addition to the mRNA in eukaryotes and a select few prokaryotes. This functions to protect the mRNA from degradation and facilitates export from the nucleus.

Reverse Transcription
Reverse transcription is essentially the copying of RNA information into a DNA form. The enzyme used to accomplish this is reverse transcriptase and can be found in retroviruses such as HIV. A retrovirus uses Reverse transcription to copy its RNA-based genetic material to DNA, which can then be integrated into the host’s genome the virus is infecting. Reverse transcription is not limited to just retroviruses, it is also used by DNA-based viruses, in eukaryotes to propagate retrotransposons and in prokaryotes when synthesizing msDNA (multicopy single-stranded DNA)

The Standard Genetic Code
The genetic code is the language by which the information coded within a nucleotide sequence is translated into peptides that ultimately form proteins. An RNA chain is divided into a series of three-nucleotide sequences known as codons codons, each of which is associated with an amino acid. The following is the standard genetic code table (though some organisms have different genetic code mappings) showing all possible three-nucleotide combinations and the related amino acid:

Degeneracy of the Code
As is apparent in the graphic above, there are far more three-nucleotide combinations than there are amino acids, so many nucleotide combinations may code for the same amino acid. This property of the genetic code is called degeneracy. Most degeneracy of the code happens at the third position in the codon, which can be explained by the wobble hypothesis. This theorizes that a single tRNA can bind to multiple different codons due to a weak pairing on the third nucleotide of the codon. In addition, degeneracy works as a simple safeguard against complications arising from genetic mutations, as some errors in replication and/or transcription will in fact code for the same protein as the undamaged DNA, thereby nullifying the effect of the error; these are commonly referred to as silent mutations. There are also special codons representing amino acids that are specifically for the start and end of translation.

Organism-Specific Modifications
Although the information displayed in the above graphic is the most commonly employed genetic code amongst organisms, there are several species that have some of their own modifications to the code. One modification in particular is that of the vertebrate mitochondrial genetic code, in which there are four instances in which a codon is translated differently than in the nuclear genetic code of the organism. Deviance from the standard genetic code is also observed in invertebrate mitochondrial codons and in the nuclear codons of several bacteria and yeasts.

Expanding the Genetic Code
Although the standard genetic code is well-known, there is still work being done to determine the subtle, organism-specific nuances of the code. For instance, recently two new amino acids, pyrrolysine and selenocysteine, have been discovered. These two residues are coded by codons that are already associated with other amino acids, but with specific mRNA signaling sequences, they may be added to the growing peptide chain during translation.

license: Creative Commons - Attribution Share-Alike - https://creativecommons.org/licenses/by-sa/4.0/


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Proteomics/Post-translational Modification/Cross-linking

Previous Section: Proteolytic Processing Next Section: Glycosylation

 * 1) Introduction
 * 2) Proteolytic Processing
 * 3) Cross-linking
 * 4) Glycosylation
 * 5) Amino Group Modification
 * 6) Carboxyl Group Modifications


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Proteomics/Post-translational Modification/Glycosylation

This Section:

= Glycosylation =

Overview
Protein Glycosylation is the post-translational process by which saccharides are selectively added to specific protein residues utilizing two distinct mechanisms in order to convey more structural stability or function to the native protein structure. Specifically this process is necessary for proper modification of a protein such that it may anchor properly into a phospholipid bilayer or is conveyed a cell signaling function resultant of the enzyme mediated addition of sugars in a site-directed manner. However due to the lack of enzyme recognition or consensus sequence knowledge, the specificity of these mechanisms occurring on peptide sequences is largely unknown. As such there is a significant amount of work that has been done in order to define prediction models for glycosylation sites in order to aid in protein modeling as a whole. One such example in specific is the pNetOGlyc 3.1 Server, developed by the Center for Biological Sequence Analysis. This utility uses neural networks to extrapolate glycosylation sites of type O-GalNAc using experimentally verified glycosylation sites and structure homology from the PDB.

Purpose
Proteins are glycosylated for several reasons. Some glycoproteins are more stable once they have polysaccharides attached, others for cell recognition and communication. Still some proteins simply refuse to fold properly without their accompanying side chains. Because glycosylation is thought to be largely a function of the Golgi apparatus, experiments into the role of glycosylation in protein conformation in vivo are difficult to design.

Roles
Glycosylation plays a critical role in the proper maintenance of protein tertiary and quaternary structure, most notably as a retainer for the intricate structure of the Fab fragment of Immunoglobulins. Specifically Immunoglobulin G utilizes as many as thirty unique glycoprotein interactions in order to create and maintain a unique Fab structure during the lifespan of the sera glycoprotein. Other functions include membrane bound recognition and adhesion activities, metabolism components, transportation duties and protein folding / mediating functions. In general, where a cellular process requires a diverse protein which must retain structural stability, a glycoprotein is usually involved.

Glycosylation and Proteomic Analysis
=Mechanisms= All forms of glycosylation are enzymatic, site specific reactions which utilize an activated nucleotide sugar. Beyond these three base requirements, several specific types of glycosylation exist.

N-Acetylglucosamine
N-linked glycosylation is the most common form of glycosylation. It is widely employed by Eukaryotes and Archaea, but rarely in Prokaryotes. This occurs through a series of steps which begin with the formation of an oligosaccharide chain consisting of around 14 sugars. This chain is then anchored on a multimer known as dolichol. Then an enzyme known as Oligosaccharyltransferase transfers the bound glycosidic chain towards the ER lumen, where it can be affixed to the nascent polypeptide being produced.

Glycosylation sequon
Glycosylation is triggered by a short sequence of amino acids known as the glycosylation sequon. This sequence is characterized by (in the N-case) an Asparagine followed by any residue except proline, followed by either Cysteine, Serine, or Threonine.

Most N-linked oligosaccharides fall into two categories which are thought to be determined by the presence sugar modifying proteins during transcription:

Complex oligosaccharides
Complexes of oligosaccharides are formed by linking multiple other types of sugars together starting with two N-Acetylglucosamine molecules. This often is terminated by the addition of sialic acid on the branching "antennae" characteristic of the chain.

High-Mannose oligosaccharides
A subset of oligosaccharides attached to secreted or membrane proteins in eukaryotic cells. They contain 5-9 mannose residues, but lack the sialic acid terminated antennae of the so called complex type.

[O-linked glycosylation]
O-linked glycosylation occurs via the addition of sugars to the Threonine and Serine residues hydroxyl-oxygen sidechains that are in close proximity to a Proline residue. O-linked glycosylation takes place typically in the Golgi apparatus. The Principal difference from the N-linked variant of protein glycosylation is the sidechain interaction variety, with type O utilizing an oxygen based linker mechanism

O-N-acetylgalactosamine (O-GalNAc)
This specific type of O-linked Glycosylation is theorized to occur in the Golgi apparatus and is simplistically characterized as further modification of the protein in late processing via addition of N-acetyl-galactosaminyltransferase to Serine or Threonine (typically Threonine) residues. This mechanism is catalyzed by the enzyme UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase and stabilized by various carbohydrates to form the complete O-GalNAc structure. This form of Glycosylation is critical for the formation of proteoglycans which is associated with extracellular matrix formation and as a component of mucosal secretions.

O-N-acetylglucosamine (O-GlcNAc)
O-N-acetylglucosamine type glycolosylation occurs as the addition of O-GlcNAc to Serine or Threonine residues if and only if phosphorylation has not occurred previously at those residues by serine or Threonine kinases. Via the mechanism of O-GlcNAc transferase, proteins glycosylated in this manner are found in both the nucleus and cytoplasm. Because of its relationship with phosphorylation sites, the recognition of Glycosylation events of this nature have significant implications in the current and ongoing cancer research that has been, up till now, centric on phosphorylation activity only. Additionally O-GlCNAc Glycosylation is a nutrient-sensing hexaosamine signaling pathway participant at the termination of the signal transduction pathway.

O-Mannose
Abundant in brain and muscle cells, this form of Glycosylation is catalyzed by O-mannose beta-1,2-N-acetylglucosaminyltransferase specific for mannose and has significant implications in Congenital Muscular Dystrophy (CMD), causing one particular disorder, specifically Duchene Muscular Dystrophy.

O-fucose & O-Glucose
These forms of Glycosylation takes place between cysteine residues in the Notch protein, an EGF signaling protein. In particular Human Notch-1 (one of four proteins in the Notch family) contains 12 O-Fucose and 17 O-Glucose sites, with the implications of improper Glycosylation resulting in abnormal development, leukemia, and Cerebral Artiopathy with Infarcts. For O-Fructose Glycosylation, the mechanism of linkage here involves GDP-fucose protein O-fucosyltransferase 1. Another mechanism of O-fucose Glycosylation involves fusion of GDP-fucose protein O-fucosyltransferase 2 to specific Thrombospondin repeats which are then selectively elongated by glucose addition. Interestingly however, both catalytic reactions occur in the Endoplasmic Reticulum, rather than in the traditional localization of glycosyltransferases in the Golgi apparatus.

C-mannosylation
C-mannosylation is a unique form of glycosylation which is characterized by the covalent bonding of alpha-mannopyranosyl to the indole second carbon of Tryptophan. Due to its incredible specificity, this form of glycosylation was not characterized until the early 1990's, and as such still remains a poorly understood mechanism with respect to its function in cellular processes.

=GPI Anchor= These membrane bound proteins are prevalent in most Eukaryotic systems and serve to regulate the release of molecules from cell surfaces and exchange of membrane molecules. Specifically they play a critical role in the recognition of enzymatic and antigenic molecules as well receptor mediated signal transduction pathways. Proteins destined for anchorage onto a membrane surface are first adhered at the carboxyterminus (c-terminal region) to a phosphodeister linkage system. This is comprised of the adsorption of phospothanolamine to a core of trimannosyl-non-acetylated Glucosamine. This Glucosamine structure is then linked to phosphatidylinositol, which is then finally adhered to the lipid bilayer via another phosphodeister linker. Solubilization of the membrane bound protein is achieved via cleavage of the phosphatidynisotil bond by Phospholipase C.

Authors
Jared Carter

Aubrey Bailey

Comparative glycoproteomics: approaches and applications
Reviewer: Corey W.

Main Focus
The finding that Post-Translational Modifications (PTMs) affect many protein sequences led to a shift in the focus of proteomics from sequences to structural and functional properties of proteins. When proteins are glycosylated it means that sugars are added to the string of amino acids which affects the structure, solubility and stability of proteins. These edits also have roles in “embryonic development, immune response and cell-to-cell interactions involving sugar-sugar- or sugar-protein-specific recognition.” Glycosylation is one PTM growing in interest because it lends itself to being used as a biomarker which has become useful in detecting prostate and breast cancer as well as some neurodegenerative diseases. This article focuses specifically on comparative glycoproteomics and its uses.

New Terms

 * Biomarker: A biomarker, or biological marker, is in general a substance used as an indicator of a biological state. (source: http://en.wikipedia.org/wiki/Biomarker)

 * Lectin: Lectins are sugar-binding proteins that are highly specific for their sugar moieties. (source: http://en.wikipedia.org/wiki/Lectin)

 * MALDI MS: Matrix-assisted laser desorption/ionization (MALDI) is a soft ionization technique used in mass spectrometry, allowing the analysis of biomolecules (biopolymers such as proteins, peptides and sugars) and large organic molecules (such as polymers, dendrimers and other macromolecules), which tend to be fragile and fragment when ionized by more conventional ionization methods. (source: http://en.wikipedia.org/wiki/Matrix-assisted_laser_desorption/ionization)

 * TOF MS: Time-of-Flight Mass Spectrometry is a method of mass spectrometry in which ions are accelerated by an electric field of known strength. This acceleration results in an ion having the same kinetic energy as any other ion that has the same charge. The velocity of the ion depends on the mass-to-charge ratio. The time that it subsequently takes for the particle to reach a detector at a known distance is measured. This time will depend on the mass-to-charge ratio of the particle (heavier particles reach lower speeds). From this time and the known experimental parameters one can find the mass-to-charge ratio of the ion.(source: http://en.wikipedia.org/wiki/Time-of-flight_mass_spectrometry)

Comparative Glycoproteomics

 * When dealing with proteins, there is a problem with the dynamic range particularly during separation. The most interesting proteins tend to be those at low concentrations. Glycoproteins, which constitute a subset of total cellular proteins, can be selectively enriched by the use of lectins. These proteins are found in plants, fungi, bacteria and animals and have an unique affinity toward carbohydrates. Lectin affinity chromatography (LAC) is based on the reversible, specific interaction of each lectin against different oligosaccharides. This method allows for the enrichment of glycoproteins and glycopeptides, but also discrimination of glycan structures as well as glycoforms of the same protein. Using lectins immobilized on a solid piece of agarose, glycoproteins can be isolated in a column. Peptide-N-glycosidase (PNGase) is then used to label the N-glycosylation site with 18O. This method is called isotope-coded glycosylation-site-specific tagging (IGOT). A mass spectrometer can clearly distinguish the resulting labeled peptides from peptides that were not isotope-coded. The major weakness of this protocol is that there is some non-specific binding can occur to non-glycosylated proteins.

Applications of Comparative Glycoproteomics

 * The functional groups found on these proteins are likely to reveal more about signaling pathways and may tell us more about mechanisms and pathogenesis of certain diseases. The use of separation techniques will also extend the dynamic range and allow us to target small subsets of proteins which will simplify systems and allow for discovery of more aberrantly glycosylated sites.

Cancer

 * Glycosylation profiles are known to change in the onset of oncogenesis. The author provides an example where up-regulation of activity of N-acetylglucosaminyltransferase V (which is responsible for the branching of N-linked glycans) has been linked to tumor invasion and metastasis in several cancers. From this knowledge of differential glycosylation in cancer cells, we can target some glycoproteins for biomarker discovery and diagnostics. In the case of better known biomarkers such as prostate-specific antigen (PSA) we may eventually be able to alter the aberrant sites for use in immunotherapy.

Neurodegenerative Diseases and Neurobiology

 * It has been shown that aberrant glycosylation might be part of the cause of Alzheimer's Disease. The change in folding of a certain protein makes a site easier to phosphorylate, but more difficult to dephosphorylate. It has also been found that glycopatterns change in Reelin, a protein used in cytoarchitectonic organization, which causes up-regulation!

Relevance to a Traditional Proteomics Course
Getting results previously mentioned used to be difficult, but with advances in structural glycobiology coupled with mass spectrometry technology experiments are getting easier to do. These new techniques allow for a more detailed view of glycosylation modifications. As more biomarkers are discovered there is hope that these types of analyses will become part of normal diagnostic routine. Putting these new types of proteomics into action will elucidate fundamental biological processes. There is also the possibility of these techniques to explain certain diseases by helping us discover these rare subsets of proteins.


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Proteomics/Protein Primary Structure/Alternative Splicing

This Section:

Alternative splicing: Biological function
Alternative splicing is the process in which the primary transcript of a gene is reorganized to produce one of multiple mature mRNA transcripts. By manipulating exonic regions, the sequence of the amino acids produced from the mRNA can be controlled, resulting in the production of different protein sequences with different structures and functions. Alternative splicing has been observed as a mechanism to produce tissue specific proteins from a single gene. This allows for increased cellular specialization without the involvement of genetic modification. This is a very critical aspect of development in that it allows the determination of cell fates in a manner that still allows for flexibility and modification. Alternative splicing has especially been studied in the context of neuronal development, however many spliced variants have been identified that are only expressed in certain tissues during development that seem to play a critical role in triggering cell-type specific gene expression.

Alternative Splicing is a major source of protein diversity in living organisms. It has been estimated that at least 30% of all genes in the human genome are alternatively spliced and this number continues to expand. It was originally thought that the number of alternatively spliced genes accounted for only 5% of proteins in humans. With the unveiling of the human genome it was revealed that the human genome contains less than 30,000 genes. This could potentially account for the huge gap between the relatively small number of genes and the vast number of proteins in the proteome.

It has been suggested that alternative splicing is the source of higher level complexity in eukaryotes. This idea is based on the thought that more complex organisms will alternatively splice their genes more often to obtain more possible mRNA sequences. However evidence shows that the level of alternative splicing between different complexities of organisms is not significant. Providing evidence of the contrary, a study was done using ESTs (expressed sequence tags ). ESTs, being a portion of a transcribed mRNA, are very effective at detecting alternatively spliced genes. As more EST studies are done, it has become apparent that there is a greater number of alternatively spliced genes than previously thought (see above).

Examples of Alternative Splicing
Alternative splicing has been implicated in several diseases. An example of a disease that plays a role in alternative splicing is Rett syndrome (RTT). This disease is found primarily in girls and is characterized by problems with forming connections between neurons, or synapses Girls with this disease typically develop normally until reaching 6-18 months. Beyond this age, they begin to show a decrease in motor and language skills that is typically accompanied by hand wringing motions. It is believed that the gene MeCP2 produces a mutant protein that disrupts its normal function as co-regulator of alternative splicing in some proteins. When this mutant version of MeCP2 is produced, a protein that lacks critical functions of the wild type is produced that does not allow regulation of alternative splicing. MeCP2 was originally identified as a methylation dependent transcriptional repressor. However it was discovered that MeCP2 has alternative functions, that was first elucidated by MeCP2's interaction with Y box binding protein (YB-1 a component of mRNPs). The complex of YB-1 and MeCP2 was shown to regulate splicing of reporter minigenes.

Microarray data from mice with mutations causing phenotypes resembling Rett showed a significant difference in the number of alternatively spliced genes vs wild type mice. Alternatively spliced transcripts matched cell-based assays which showed MeCP2's role in cassette exon changes.

Splicing Mechanism
Splicing occurs through the mechanism of the Spliceosome, a complex composed of a number of proteins and snRNA's. including the snRNAs U1, U2, U3, U4, U5 and U6. These snRNAs recognize the splice sites and then recruit other proteins that connect the splice sites. These splice sites are then brought together through the interaction of these proteins which form the spliceosome. Once the spliceosome has formed, the sites are cleaved to bring the correct exons (or introns) together. Splice sites in organisms have not been well characterized. Some progress has been made in the area of computational prediction using HMM profiling and other forms of machine learning. This will be discussed later in this article. The 5' end of an intron is characterized with a consensus sequence most commonly ending in "GU". This region is known as the splice donar site. The 3' end of an intron is known as the splice acceptor site and contains a consensus sequence with an AG at the intron/exon boundry. There is also an adenine, usually close to the 3' end of an intron, known as the branch point that plays a role in the splicing mechanism. During splicing, U1 begins the formation of a complex at the splice donor site, while U2 recruits portions of the spliceosome complex to the splice acceptor site. U4, U5, and U6 bridge the gap between these two sites, causing the intron to fold. The DNA is digested, at the splice donar site. This portion of the intron is then ligated to the branch point, forming a lariat. This brings the exonic regions is close proximity to each other, allowing for ligation. Finally, the splice acceptor site is cut and the exonic regions are joined.

There are 4 common types of alternative splicing, they are as follows:

 * Alternative promoter selection: A different promoter is used for different splice variants. This results in a different start of the mRNA transcript.

 * Alternative selection of cleavage/polyadenylation sites: Different exons are spliced based on recognition of different cleavage or polyadenylation sites, entire exons can be skipped.  Results in a different exon at the 3’ end of the transcript.

 * Intron retention: Introns are used as coding regions. A sequence that is normally considered an Intron is retained in the final transcript that serves as a template for translation.
 * Exon cassette: Entire exons can be skipped in the middle of the protein, resulting in a different transcript

The Growing Need for Protein Identification:
Proteins are the basic unit of structure and function within living systems. Consequently the field of proteomics has taken on added significance in the modern study of biology. The genomic revolution, which culminated in the sequencing of many genomes, has generated a tremendous amount of data. The field of proteomics has unfortunately been lagging behind, resulting in a disconnect between genomic information and observable phenotypes. Originally, proteins and protein dependent pathways were studied individually. Recently an emphasis on systems biology has lead to changes in this methodology. Entire cells are being characterized with high throughput techniques.

Mass Spectrometry has become the gold standard of protein identification. Briefly, proteins are broken down into peptides, suspended into a gas phase by one of a various number of methods, ionized, and sent through a detector which can determine the mass to charge ratio of various peptides. Mass spectroscopy can be easily automated and combined with other forms of protein separation, making it an ideal candidate for high throughput analysis. In addition, thousands of peptides can be identified from a single source at one time, making this technique much more applicable to systems biology then older techniques such as Edman degradation. Mass spectroscopy can also be used to identify single proteins of interest that have been isolated using other techniques, such as chromatography.

Splicing and Protein Identification
A major drawback of mass spec analysis, and even identification by Edman degredation, is that proteins must be digested into peptides before identification. Often for use with shotgun sequencing , proteins are digested before any form of isolation process is done. In order to confirm identifications protein databases are searched in order to match unique peptides to entire proteins. This process is made more complicated by the immense level of sequence homology shared by peptides produced by alternative splicing. . These proteins, although sharing similar primary structures may have very different or even antagonistic functions, making their identification critical from a biological perspective. What is more, the level of alternative splicing that occurs is not well characterized so it is not even well known which proteins cannot be unambiguously identified. These problems will likely remain until alternative splicing is well documented or can be predicted efficiently computationally.

Effects to analyze alternative splicing:
In vivo analysis is currently the most accurate way to identify alternative splicing, either at the transcript, or in some cases at the protein level. Numerous databases exist that document proteins known to undergo alternative splicing, including the Alternative Splicing Database, and the Transcript Diversity database. While these are good references, as discussed above, the estimates of even the amount of alternative splicing present in eukaryotic organisms vary dramatically. There is, therefore, very little information on how complete these databases are. Steps have also been taken to computationally predict alternative splicing. Generally these algorithms combine gene finding approaches with experimental data. Splice sites are recognized and rated in efficiency based on consensus sequences. Sequences are then matched to known expressed sequence tags to make predictions. Tools such as BLAST, Spidey, and SIM4 can be adapted for these processes. Most modern computational tools encounter difficulty in comparing genomic data to sequences as small and variable as splice sites. False positives and negatives are fairly common. New approaches are still being developed.


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Proteomics/Post-translational Modification/Carboxyl Group Modifications

Chapter written by: Rhea Sanchez and Ashlee Benjamin

Contact ris6859@rit.edu or amb4541@rit.edu for contributions

This Section:

Carboxyl Group Modifications
Nearly all polypeptides undergo modifications after being translated from mRNA. Many types of these modifications occur at the ends of the polypeptide. The C-terminus of a protein or polypeptide is the end of the amino acid chain terminated by a free carboxyl group (-COOH).

There are several ways in which the C-terminus of the polypeptide can be modified post-translationally. The most common post-translational modification is the addition of a lipid anchor to the C-terminus. This modification allows the protein to be anchored within the membrane without having a transmembrane domain.

Types of C-terminal Modification
There are several types of C-terminal modification including: amidation, prenylation, glypiation, ubiquitination, sumoylation, and methyl/ethyl-esterification.

Amidation
C-Terminal amidation is a common posttranslational modification in peptide hormones. Amidation is the addition of an amide group to the end of the polypeptide chain.

The amide group for C-terminal amidation is contributed by a Glycine residue. This Glycine is present in a precursor C-terminal sequence that resembles XGXX, where X represents any amino acid. When digesting the polypeptides with proteases like CpY (carboxypeptidase Y), CpA and CpB, CpY releases the C-terminal amides, but CpA and CpB do not. Amidation neutralizes negative charges on the C-terminus of the polypeptide. Peptidylglycine α-hydroxylating monooxygenase and peptidyl α-hydroxyglycine α-amidating lyase are two enzymes associated with amidation, and both of which are encoded by the same gene: Peptidylglycine α-amidating monooxygenase.

Peptidylglycine α-amidating monooxygenase, or PAM, precursor encodes a multifunctional protein that can be divided into three parts. First, the NH2-terminal third of the PAM precursor contains the enzyme peptidylglycine α-hydroxylating monooxygenase, or PHM. Secondly, the inner third of the PAM precursor contains the enzyme peptidyl α-hydroxyglycine α-amidating lyase, or PAL. Finally, the COOH-terminal third of the PAM precursor encodes a transmembrane domain and a hydrophilic domain that may form a cytoplasmic tail.

Both activities successively catalyze the production of α-amidated peptides from their glycine-extended precursors in a two-step process.

Prenylation
Prenylation (also isoprenylation or lipidation) is the post-translational addition of hydrophobic molecules, called prenyl groups, to a protein. The process of prenylation is catalyzed by three enzymes: Farnesyltransferase and Geranylgeranyltransferase I and Geranylgeranyltransferase II.

Farnesyltransferase and Geranylgeranyltransferase I are structurally and functionally similar proteins. In terms of structure, both enzymes consist of two subunits: the α-subunit and the β-subunit. Both enzymes recognize the CAAX (C represents Cysteine; A represents an aliphatic amino acid; X represents any amino acid) box at the C-terminus of the target protein. Depending on the enzyme, either a farnesyl-isoprenoid or geranylgeranyl-isoprenoid membrane anchor is added to the cysteine residue of the CAAX box near the C-terminus. Geranylgeranyl transferase II, or Rab geranylgeranyltransferase, catalyzes a reaction in which geranylgeranyl groups are added to cysteine residues located near and/or at the C-terminal end of Rab proteins. However, due to the hypervariability of the C-termini of Rab proteins, Rab proteins do not have a consensus sequence, such as the CAAX box, which the Rab geranylgeranyl transferase can recognize. Thus, Rab proteins recruit the help of Rab escort proteins, or REP, which can then be recognized by the Rab geranylgeranyltransferase. After prenylation, the Rab proteins become insoluble due to the action of lipid anchors. REP is partially responsible for binding the geranylgeranyl groups and rendering them soluble. REP also transports the Rab protein to the appropriate membrane.

Glypiation
The C-terminus of the peptide consists of hydrophobic amino acids. The hydrophobic end of the peptide undergoes a proteolytic cleavage, and a glycosylphosphatidylinositol, or GPI anchor, is added to the C-terminus. This process is known as glypiation. Enzymes called phospholipases then release the GPI-linked proteins. Phospholipase C is an enzyme known to hydrolyze the phosphodiester bond of the phosphatidylinositol found in GPI-anchored proteins, resulting in the release of the mature protein. GPI-anchors play a critical role in receptor-mediated signal transduction pathway. Thus, it is to no surprise that defects in the glypiation process or in phospholipase-catalyzed reaction can have dire effects on the organism. One condition associated with defective GPI anchors is the disease known as paroxysmal nocturnal hemoglobinuria

Ubiquitination
Ubiquitination, or ubiquitylation, is the process of covalently attaching one or more ubiquitin monomers via an isopeptide bond. Ubiquitination is most notably associated with targeting substrates for degradation by the 26S proteosome. However, it has also been linked to post-translational protein localization, activity, conformation, and protein-protein interactions.

The precise role ubquitination plays in the fate of a protein is believed to depend on the length of the ubiquitin chain appended to the protein. Monoubiquitination is the attachment of a single ubiquitin monomer to a protein, a non-proteolytic signal involved in endocytosis, virus budding, endosomal sorting, DNA repair, histone regulation and export from the nucleus. Seven lysine residues in ubiquitin affect its ability to attach other ubiquitin molecules. This process of attachment is known as polyubiquitination. The best-studied examples are chains of four polyubiquitins linked through the Lysine residue at postion 48. These ubiquitins target proteins for degradation.

Deubiquitinating enzymes, or DUBs, can, however, can undo the modification by cleaving off the ubiquitin protein(s). Several disorders have been linked to ubiquitination including Angelman syndrome, Von Hippel-Lindau syndrome, Liddle's Syndrome, and Fanconi anemia.

Sumoylation
Small Ubiquitin-related Modifier proteins, or SUMO proteins, are small proteins that covalently attach to proteins in a process known as sumoylation. As its name suggests, SUMO proteins and ubiquitin are similar proteins sharing many characteristics including the sequence of enzymatic reactions directing either process. However, unlike ubiquitin, SUMO proteins do not act as proteolytic signals. SUMOylation has been associated with various cellular functions and processes including cell cycle regulation, DNA repair, chromosomal maintenance, modifying cytoplasmic signal transduction, nuclear import and subnuclear compartmentalization, DNA repair, transcription regulation,and stress response.

Methyl-Esterification
Methyl esterification involves the conversion of carboxylic acids to methyl esters. Methyl esterification has been associated with the membrane localization of proteins including small G proteins. Carboxyl methyl esters have also been linked to rendering peptides resistant to exopeptidases.

Function
Post-translational modification of the Carboxyl terminus of a polypeptide has been linked to many biological functions and processes as listed below:
 * Peptide activation
 * Membrane integration
 * Localization
 * Activity
 * Structure
 * Protein-protein interactions
 * Proteolytic signalling
 * Endocytosis
 * Endosomal sorting
 * Histone regulation
 * DNA repair
 * Virus budding
 * Nuclear export
 * Cell cycle regulation
 * Chromosomal maintenance
 * Modifying cytoplasmic signal transduction
 * Nuclear import and subnuclear compartmentalization
 * Transcription regulation
 * Stress response


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Topfield 5800/Stable Toppy

Chunkywizard's Guide to a Stable Toppy

 * Firmware : Load on the Toppy.org.uk recommended firmware (currently 5.13.65). Although this is fairly stable it can be improved by patching it.  There are a number of bug fixes; I would recommend the following patches as a minimum: 1365BfBqCeCyDeEcErEsFGmHMhNfPPcPfRReRpRsSSrStT2XpXw. A pre-built copy of this firmware can be download from here. Note if you are running EPG Navigator and UK Auto Scheduler you may want to drop the De patch as it is not supported by these TAPs.
 * Channels : Check that the channels are correct. They should be as per this channel list. Check you have no duplicate channels and no channel numbers in the 1000's. If you have then consider using the ChannelManager TAP or the newer Channel Organiser TAP to sort this out. Note that if you have used ChannelManager and used the option to renumber regional variants, you may have additional channels (typically in the 200+ range).
 * Signal : Check that your signal strength is acceptable. Try to get 100% quality across all muxes and above 60% strength. If you are unsure of your signal strength then use the SignalMonitor TAP or the manual Service Search in the Installation Menu (see here for details about how to do a manual scan, and then sit back and watch the real-time display — press the Red button on this screen you get a bigger display that beeps a lot).
 * TAPs : If you are using TAPs then make sure they are all up to date (using the latest stable release), use the default configurations where possible, and try only to use mainstream, UK supported ones (so help can be provided on the UK Forums if issues occur). Fewer are better, in my opinion.
 * Interactive Services (MHEG) : The MHEG engine (used for the "red button" Interactive Services) on the Toppy is known for being of dubious quality. While 5.13.65 has the best implementation of this, it is still an area of concern. If you want to be extra careful consider turning off MHEG in the main menu. If you wish to use it (for radio for example) but wish to protect yourself then consider a TAP like MHEGControl.
 * Some Light Reading : Check the manual for the Toppy (and for the individual TAPs you use), and consult (and search) the UK Forums for any issues for the setup you have. Some interactions are well known and documented, and this will save you a lot of time and swearing. Also, browse through the Troubleshooter for some help on common problems.

title: Topfield 5800/Stable Toppy


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User talk:Christopher.fucile

Welcome!
Welcome, !

Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.-- – Mike.lifeguard  | talk 23:02, 12 March 2008 (UTC)

title: User talk:Christopher.fucile


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User talk:Dfsurdyk

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title: User talk:Dfsurdyk


text:
User talk:Commander crash

Welcome!
Welcome, !

Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.-- – Mike.lifeguard  | talk 23:12, 12 March 2008 (UTC)

title: User talk:Commander crash


text:
User talk:117.97.5.195

Join Us!
-- – Mike.lifeguard  | talk 23:12, 12 March 2008 (UTC)

title: User talk:117.97.5.195


text:
User talk:Cziska

Welcome!
Welcome, !

Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.-- – Mike.lifeguard  | talk 23:54, 12 March 2008 (UTC)

title: User talk:Cziska


text:
Template talk:Altaic languages

Japanese and Korean
The inclusion of Japanese (likewise Korean) in the Altaic language group is controversial and not generally accepted, AFAICT.

I suggest we accord with consensus, as in: Specifically:
 * Classification of the Japanese language
 * Classification_of_the_Japanese_language

Nbarth (talk) 23:59, 12 March 2008 (UTC)

 * Pursuant to above, I suggest we stay in sync with:
 * w:Template:Altaic languages
 * ...and not include the template on Japanese or Korean.
 * Nbarth (talk) 00:03, 13 March 2008 (UTC)

 * I've also added a caveat; I suggest we either include the caveat, or don't include Japanese and Korean.
 * Nbarth (talk) 00:08, 13 March 2008 (UTC)

To say it is "Not generally accepted" (or conversely, to say it "IS generally accepted") is not NPOV. I've reworded it to acknowledge the controversy, without taking a side either way. Manning Bartlett (discuss • contribs) 05:52, 8 December 2011 (UTC)

title: Template talk:Altaic languages


text:
First Aid/Manual of Style

Terminology

 * How do we refer to "the injured person"
 * We decided to use victim for the book proper, and either victim or patient in the ../Advanced Topics/ chapter. Casualty is not used.

 * CPR or BLS?
 * CPR is used more prominently because that is how the public knows the technique. BLS is acceptable, but should be avoided outside the ../Advanced Topics/ chapter.

 * C stands for Compressions
 * Due to changes introduced in the 2005 standards, C no longer stands for Circulation, but rather for Compressions. This is because there is no circulation check for lay rescuers, and this change in terminology reinforces the new procedures.

Scope & audience
The intended audience for this book is people (primarily young people in high school or college/university) who are taking a Standard First Aid with CPR-C course - that is, this book covers only lay rescuer procedures and will not deal with healthcare provider procedures. This is based on an international consensus for training. Where major regional variations (particularly in resuscitation) exist, they should be noted.

Standard First Aid with CPR-C includes:
 * 1) Goals of first aid
 * 2) Legal implications of first aid (consent, liability and abuse)
 * 3) Self-protection
 * 4) Anatomy and physiology of ABC priorities
 * 5) Assessment (primary & secondary)
 * 6) One-rescuer and two-rescuer CPR (adult & child & infant) (complete & summary)
 * 7) Obstructed airway: conscious victim (adult & child & infant)
 * 8) Obstructed airway: unconscious victim (adult & child & infant)
 * 9) Management of bystanders
 * 10) Respiratory emergencies: asthma/hyperventilation
 * 11) Circulatory emergencies: shock, heart attack/angina, external bleeding, stroke/TIA
 * 12) Care of unconscious victim
 * 13) Suspected spinal injury
 * 14) Environmental emergencies: heat & cold illness
 * 15) Bone or joint injury
 * 16) Abdominal or chest injury
 * 17) Burns
 * 18) Facial injury
 * 19) Seizure
 * 20) Diabetes
 * 21) Poisoning
 * 22) Critical incident stress management

Spelling & conventions

 * Canadian English is dominant, and for consistency's sake, should be used whenever possible.
 * Language should avoid being overly technical, and should attempt to present analogies or simplified explanations or mnemonics whenever possible. While there is massive amounts of scientific evidence or practical experience behind the reasoning for any given technique, it's usually not necessary to present any of that background information. When explanation is needed, practical reasons are preferred, as they'll be easily remembered, and will help the reader in the practical component of their course.
 * There are a series of templates which should be used to highlight key points, etc.
 * Images should be used to illustrate concepts wherever practical.

title: First Aid/Manual of Style


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title: User talk:Stepshep


text: User talk:68.109.151.82

title: User talk:68.109.151.82


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User talk:Ilovemyyukon

Welcome!
Welcome, !

Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.--Whiteknight (Page) (Talk) 02:19, 13 March 2008 (UTC)

I added the tag for you...
You added Living With a Narcissist to VfD but forgot to tag it, just to let you know I did it for you... --Panic (talk) 14:00, 13 March 2008 (UTC)

title: User talk:Ilovemyyukon


text:
C++ Programming/Code/Standard C Library/Functions/memchr

memchr
The memchr function looks for the first occurrence of ch within count characters in the array pointed to by buffer. The return value points to the location of the first occurrence of ch, or NULL if ch isn't found. For example:

 * Related topics: memcmp - memcpy - strstr


text:
C++ Programming/Code/Standard C Library/Functions/memcmp

memcmp
The function memcmp compares the first count characters of buffer1 and buffer2. The return values are as follows:

 * Related topics: memchr - memcpy - memset - strcmp


text:
C++ Programming/Code/Standard C Library/Functions/memcpy

memcpy
The function memcpy copies count characters from the array from to the array to. The return value of memcpy is to. The behavior of memcpy is undefined if to and from overlap.

 * Related topics: memchr - memcmp - memmove - memset - strcpy - strlen - strncpy


title: Category:Book:Eac3to


text: User talk:210.10.140.124

title: User talk:210.10.140.124


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User talk:Basuindranil 84

Welcome message
Welcome, !

Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally. Webaware talk 07:49, 13 March 2008 (UTC)

title: User talk:Basuindranil 84


text:
User talk:212.219.143.131

Welcome!
Welcome to Wikibooks, a collection of open-content textbooks! You don't have to log in to read or edit articles on Wikibooks, but creating an account is quick, free and non-intrusive, requires no personal information, and gives you many benefits, including:
 * The use of a username of your choice
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We hope that you choose to become a Wikibookian and create an account. Feel free to ask me any questions you may have on my talk page. By the way, make sure to sign your posts and comments with four tildes (~~~~), which will let others know who left it.

I reverted your edit to Analog and Digital Conversion/Analog vs Digital because, while I realize that "analogue" is the correct British spelling, the title of the book uses American spellings, so we should probably keep consistency. Thanks, Νεοπτόλεμος ( talk | email | contribs ) 10:03, 13 March 2008 (UTC)

title: User talk:212.219.143.131


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title: User talk:217.206.228.72


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User:Chrisdone~enwikibooks

Hi, my name's Chris Done. E-mail: chrisdone@gmail.com Web site: http://chrisdone.ath.cx/

title: User:Chrisdone~enwikibooks


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User talk:Sehgalthegreat

Welcome!
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Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.--Whiteknight (Page) (Talk) 12:39, 13 March 2008 (UTC)

title: User talk:Sehgalthegreat


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User talk:Gaspirc

Emergency Operation Centre GIS
G'day, this book has been listed for possible deletion, as it is probably better suited to Wikiversity. Please make comments on this book at Votes for deletion. Webaware talk 13:49, 13 March 2008 (UTC)

I agree - how do you move it to wikiUni?

The project will be starting up again in sept 2008

title: User talk:Gaspirc


text:
Talk:The Rowers of Vanity Fair/Some Editors Authors and Artists of Vanity Fair

This article makes reference to Bertram Fletcher Robinson, rowing and Vanity Fair. There are both errors and omissions in the article. For example, BFR died aged 36 years and he was a member of the 1894 Cambridge University Trial VIII. He also edited a book entitled Rowing that was written by RC Lehmann and co-authored another entitled Rowing and Punting (The Isthmian Library and Suffolk Sporting series respectively).

Please see the following links for a fuller discussion about BFR and his relationship with RC Lehmann and other notable rowers:

Regards,

Paul Spiring.


text:
Technical Book Development/Learning Styles

Learning styles have been the subject of much research and debate. A number of questionnaries have been designed to analyses individual learning styles.

 * Overview

Diagrams

 * Kolb Learning Cycle

Learning Style Questionnaires

 * Felder and Soloman - online
 * Honey and Mumford - published


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title: User talk:Cxw


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C++ Programming/Code/Standard C Library/Functions/strstr

strstr
The function strstr returns a pointer to the first occurrence of str2 in str1, or NULL if no match is found. If the length of str2 is zero, then strstr will simply return str1.

For example, the following code checks for FPIFCthe existence of one string within another string: JHJH-C´(J"JC

When run, the above code displays this output:

Found a substring: 'a string of characters'

 * Related topics: memchr - strchr - strcspn - strpbrk - strrchr - strspn - strtok


text:
C++ Programming/Code/Standard C Library/Functions/strchr

strchr
The function strchr returns a pointer to the first occurrence of ch in str, or NULL if ch is not found.

 * Related topics: strcat - strcmp - strcpy - strlen - strncat - strncmp - strncpy - strpbrk - strrchr -strspn - strstr - strtok


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C++ Programming/Code/Standard C Library/Functions/strcat

strcat
The strcat function concatenates str2 onto the end of str1, and returns str1. For example:

Note that strcat does not perform bounds checking, and thus risks overrunning str1 or str2. For a similar (and safer) function that includes bounds checking, see strncat.

 * Related topics: strchr - strcmp - strcpy - strncat


text:
Technical Book Development/Learning Strategies

Learning strategies are the approaches we use to learn a new subject. A good strategy would be based on an understanding of one's own learning style, the range of learning resources available and the objective of the learning task

Learning involves a number of activities as one moves from newbie to expert.

Doing
Experiential learning is learning by doing - but what do we do? How do we choose what to do?

Digesting
Reflection and consolidation of the experiences of doing -

Feedback
How do know what we know? How do we assess the quality of our understanding

Contributing
Learning on the Web involves interaction as one learns - initially with questions, later with contributions

Strategy involves the scheduling of these learning activities, deciding how much time to spend on each and when to move on


text:
User talk:Aldur~enwikibooks

Welcome!
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Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.--Whiteknight (Page) (Talk) 16:55, 13 March 2008 (UTC)

Your account will be renamed
Hello,

The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

Unfortunately, your account clashes with another account also called Aldur. To make sure that both of you can use all Wikimedia projects in future, we have reserved the name Aldur~enwikibooks that only you will have. If you like it, you don't have to do anything. If you do not like it, you can pick out a different name.

Your account will still work as before, and you will be credited for all your edits made so far, but you will have to use the new account name when you log in.

Sorry for the inconvenience.

Yours, Keegan Peterzell Community Liaison, Wikimedia Foundation 22:55, 17 March 2015 (UTC)

Renamed
 This account has been renamed as part of single-user login finalisation. If you own this account you can |log in using your previous username and password for more information. If you do not like this account's new name, you can choose your own using this form after logging in: . -- Keegan (WMF) (talk) 04:30, 19 April 2015 (UTC)

title: User talk:Aldur~enwikibooks


text:
User talk:Livetorow

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Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally. -- Herby talk thyme 17:12, 13 March 2008 (UTC)

title: User talk:Livetorow


text:
Cookbook talk:Sachertorte

Is it difficult?
is this recipe hard to make? because im only 14 and i'm in my skills for living class aand we are creating resteraunts for different countrys. i might make this recipe. —Preceding unsigned comment added by 205.196.178.196 (discuss • contribs)

 * G'day, I've never made this cake myself (because I don't make cakes), but the recipe summary box says that it is a very difficult recipe (5/5). Reading it, I'd say it's probably just difficult (4/5). Perhaps you could look at trying some of the other cake recipes first - for example, 1-2 Chocolate Cake and 1-2-3-4 Cake look quite easy, and tasty. Webaware talk 02:23, 14 March 2008 (UTC)

It's not really that difficult, it's just a frosted chocolate cake. Make sure to have all the ingredients (at room temperature) ready beforehand.

I have to agree that it's not really difficult. Most of skills needed are the same as for a chocolate mousse.

title: Cookbook talk:Sachertorte


text:
Wikibooks:Requests for deletion/Learn Linspire

== Learn Linspire ==

This is a soft redirect that now points to a page filled only with advertisements. It seems to be protected so I can not add a speedy tag, but I think this is really a case for speedy deletion. Thenub314 (talk) 09:36, 7 August 2009 (UTC) Thenub314 (talk) 09:36, 7 August 2009 (UTC)

There was actually a VFD on this previously.

I personally do not care for soft redirects. Google can index all the pages on the Internet and point to them. Wikibooks doesn't need to. I feel that this is a speedy delete as well. -- Adrignola talk contribs 12:39, 7 August 2009 (UTC)
 * As good web citizens, we aim not to break links. Your personal dislike (or mine) for soft redirects doesn't make deleting them a good idea in all cases; you'll need to explain why this one shouldn't be kept. — Mike.lifeguard | talk 00:57, 8 August 2009 (UTC)

 * Symbol delete vote.svg Link broken with no forwarding address. Geoff Plourde (talk) 01:17, 8 August 2009 (UTC)

Delete No meaningful content. --Swift (talk) 19:11, 16 August 2009 (UTC)


text:
Wikibooks:Requests for deletion/LIL German 1

LIL German 1
{| cellspacing="5" cellpadding="5" style="border: 1px red solid; background: #ffffcc; width: 95%; margin: auto; color: #000000;" | style="width: 40px; text-align: center;" | | Closed as delete all – Mike.lifeguard  | talk 17:50, 13 March 2008 (UTC) |- | colspan="2" style="border-top: 1px red dashed;" |

This is content that would, in correct form, belong on a user page. It is a letter for help on this book, when we already accomplish the job pretty well with German. I suggest that this book ought to be deleted. Thoughts? Laleena (talk) 13:32, 3 March 2008 (UTC)

 * - really just an advert for someone else's book -- Herby talk thyme 13:51, 3 March 2008 (UTC)
 * [[Image:Symbol delete vote.svg|15px]] Delete - this is an ad. No thanks. – Mike.lifeguard  | talk 01:37, 4 March 2008 (UTC)
 * There was discussion about this book last June, see Languages bookshelf, where the author said they could not convert the book from RTF to wiki format themselves but hoped to do so with assistance. Regrettably, with no sign of progress since then, it is probably time to delete it. Recent Runes (talk) 12:18, 4 March 2008 (UTC)
 * And I would like to add LIL Esperanto 1 and LIL French 1 into this VfD as well, since they are virtually identical, created around the same time by the same contributor, and having also not progressed at all since they were first created. --Whiteknight (Page) (Talk) 01:16, 5 March 2008 (UTC)
 * [[Image:Symbol comment vote.svg|15px]] Comment Why don't you put them up, then, in a separate section? Laleena (talk) 01:29, 5 March 2008 (UTC)
 * [[Image:Symbol comment vote.svg|15px]] Comment Agree w/ WK - those other 2 should be deleted too. – Mike.lifeguard  | talk 19:17, 5 March 2008 (UTC)
 * [[Image:Symbol comment vote.svg|15px]] Comment Agree w/ WK - --Panic (talk) 14:12, 6 March 2008 (UTC)

 * [[Image:Symbol delete vote.svg|15px]] Speedy Delete - There really isn't any value to this content existing in the main Wikibooks namespace, and in fact is somewhat harmful to the project in terms of using this website as a webhosting/advertising venue. We certainly don't want to see a precedent for more pages like this to pop up. I don't object to somebody putting links of this nature on their user page or making a reasonable effort to request assistance on the Reading Room pages, but it simply doesn't belong in this format as if it were a wikibook.  I very nearly just hit the delete button on this myself.  --Rob Horning (talk) 16:16, 7 March 2008 (UTC)
 * per Rob. Νεοπτόλεμος ( talk | email | contribs ) 23:31, 7 March 2008 (UTC)

LIL Esperanto 1
This one is split off from the above LIL German 1 entry and is nominated for the same reasons. Laleena (talk) 22:50, 6 March 2008 (UTC)
 * per LIL German 1 above. Νεοπτόλεμος ( talk | email | contribs ) 23:31, 7 March 2008 (UTC)

LIL French 1
This is another of the "LIL" language books that are more advertisement than anything. Νεοπτόλεμος ( talk | email | contribs ) 23:31, 7 March 2008 (UTC)
 * - per the above LIL German 1 nomination. Laleena (talk) 01:56, 8 March 2008 (UTC)

 * }


text: Wikibooks:Requests for deletion/Gears of War Comprehensive Guide


text: User talk:Jignesh29

title: User talk:Jignesh29


text: User talk:89.165.193.52

title: User talk:89.165.193.52


text: User talk:Net surfer

title: User talk:Net surfer


text: User talk:205.196.178.196

title: User talk:205.196.178.196


text: User talk:Snowolf

title: User talk:Snowolf


text:
User talk:87.5.12.250

Join Us!
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title: User talk:87.5.12.250


text: User talk:66.244.203.153

title: User talk:66.244.203.153


text:
Cookbook:Coconut Chicken

The original contributor provided the following anecdote:"'On a recent trip to the Caribbean I was impressed by all the roadside Barbecue stops that spring up on weekends, where you can buy, very cheaply, a portion of chicken, usually in a good, if rather sticky barbecue sauce, to take away and eat on a wonderful beach somewhere! I jokingly suggested to one enterprising young man, that he also offer chicken marinaded in coconut, herbs and spices as an alternative. He tried it and told me that evening that he had had almost more customers for this recipe, than for his barbecued chicken. It may become all the rage in the future!! It certainly is delicious!'"

Marinating

 * Skin-on chicken legs, breasts, or wings (sufficient for the number of people you are cooking for)
 * 1 tin (400 ml) coconut milk
 * 1 lime, zested and juiced
 * 1 bunch fresh mint, chopped
 * 1 large sprinkle of paprika
 * 1 pinch of salt
 * 1 small knob of fresh ginger, grated

Rice

 * 1 cupful of basmati rice per person
 * 10 g butter (optional)
 * 3 cloves

Marinating

 * 1) Stab the chicken in various places to a depth of about ½ inch so that they take on the taste from the marinade.
 * 2) Combine all the contents of the marinade together in a dish, and place the chicken into it so that the chicken is covered by the marinade. Let marinate, turning occasionally, for at least 3 hours, or overnight is possible—the longer the better.
 * 3) Place the chicken pieces on a barbecue, an electric grill, or even in the oven. Cook until done, making sure you coat the chicken with plenty of the marinade as you cook. You should aim for a nice crispy skin.

Rice

 * 1) In a large saucepan bring some salted water to a boil, and add the cloves.
 * 2) Add the rice, and boil until the rice is cooked. Drain and rinse under hot water to remove excess starch. Take out the cloves and discard.
 * 3) Return the rice to the pan and place over a low heat. Add about ½ cupful of the coconut marinade mixture (or any leftover coconut milk from the tin) to the rice, and heat through slowly.
 * 4) Add the butter at the last minute, and let it melt. If there is any left over, also add a handful of the chopped mint leaves to the rice as well.
 * 5) Fluff up the rice with a fork.

Serving

 * 1) Place rice in the middle of your serving plate, place the grilled/barbecued chicken on top, sprinkle with a squeeze of fresh lime juice, and serve with a green salad.

Notes, tips, and variations

 * You can roast some bananas in the same oven to go with this, either in their skins, or in foil with a little cinnamon!

title: Cookbook:Coconut Chicken


text: Wikibooks:Requests for deletion/Halo 3

title: Wikibooks:Requests for deletion/Halo 3


text: Wikibooks:Requests for deletion/AP European History


text:
User talk:AiM~enwikibooks

Welcome!
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Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally.-- – Mike.lifeguard  | talk 20:34, 13 March 2008 (UTC)

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Hello,

The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

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title: User talk:AiM~enwikibooks


text:
User talk:CiveM

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title: User talk:CiveM


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User talk:Qaisar Mehmood~enwikibooks

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The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

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Yours, Keegan Peterzell Community Liaison, Wikimedia Foundation 23:38, 17 March 2015 (UTC)

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title: User talk:Qaisar Mehmood~enwikibooks


text:
User talk:Mutlashi~enwikibooks

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Hello,

The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

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title: User talk:Mutlashi~enwikibooks


text:
User talk:Nets

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title: User talk:Nets


text:
User talk:The Obento Musubi

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title: User talk:The Obento Musubi


text:
User talk:Zamani11594

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title: User talk:Zamani11594


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User talk:Zamani2008

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title: User talk:Zamani2008


text:
User talk:Wikisoldier~enwikibooks

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The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

Unfortunately, your account clashes with another account also called Wikisoldier. To make sure that both of you can use all Wikimedia projects in future, we have reserved the name Wikisoldier~enwikibooks that only you will have. If you like it, you don't have to do anything. If you do not like it, you can pick out a different name.

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Yours, Keegan Peterzell Community Liaison, Wikimedia Foundation 23:54, 17 March 2015 (UTC)

Renamed
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title: User talk:Wikisoldier~enwikibooks


text:
User talk:DieselSandwich

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Simple remark
I've been patrolling your page creations and noticed that most are empty of real content and only have navigational helpers, in it self there is no problem with that but doing the page creation this way prevents real patrolling for vandalism or defacement to occur (since pages are put on the patrolling list on creation for validation). Can you delay adding navigational helpers after or at the same time some content is added ? This would also help any wannabe contributor to the project to see that content is missing looking only to at the TOC. --Panic (talk) 20:32, 3 November 2008 (UTC)

(This issue was resolved after discussion and after the class I was TA for filled in the content required) --DieselSandwich

title: User talk:DieselSandwich


text:
User talk:Adnankhan17

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title: User talk:Adnankhan17


text:
User talk:Srigbhat

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title: User talk:Srigbhat


text:
User talk:Sripathi~enwikibooks

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The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

Unfortunately, your account clashes with another account also called Sripathi. To make sure that both of you can use all Wikimedia projects in future, we have reserved the name Sripathi~enwikibooks that only you will have. If you like it, you don't have to do anything. If you do not like it, you can pick out a different name.

Your account will still work as before, and you will be credited for all your edits made so far, but you will have to use the new account name when you log in.

Sorry for the inconvenience.

Yours, Keegan Peterzell Community Liaison, Wikimedia Foundation 23:47, 17 March 2015 (UTC)

Renamed
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title: User talk:Sripathi~enwikibooks


text:
User talk:Inky~enwikibooks

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Hello,

The developer team at Wikimedia is making some changes to how accounts work, as part of our on-going efforts to provide new and better tools for our users like cross-wiki notifications. These changes will mean you have the same account name everywhere. This will let us give you new features that will help you edit and discuss better, and allow more flexible user permissions for tools. One of the side-effects of this is that user accounts will now have to be unique across all 900 Wikimedia wikis. See the announcement for more information.

Unfortunately, your account clashes with another account also called Inky. To make sure that both of you can use all Wikimedia projects in future, we have reserved the name Inky~enwikibooks that only you will have. If you like it, you don't have to do anything. If you do not like it, you can pick out a different name.

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Sorry for the inconvenience.

Yours, Keegan Peterzell Community Liaison, Wikimedia Foundation 23:14, 17 March 2015 (UTC)

Renamed
 This account has been renamed as part of single-user login finalisation. If you own this account you can |log in using your previous username and password for more information. If you do not like this account's new name, you can choose your own using this form after logging in: . -- Keegan (WMF) (talk) 05:03, 19 April 2015 (UTC)

title: User talk:Inky~enwikibooks


text:
User talk:Voyaging

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title: User talk:Voyaging


text:
User talk:PhoenixBlitzkrieg

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title: User talk:PhoenixBlitzkrieg


text:
Wikijunior talk:Animal Alphabet/B

This is not a bat, but a flying fox.... fix it. —The preceding unsigned comment was added by 130.89.163.149 (talk • contribs).
 * A flying fox is a species of bat. There is nothing to fix. --Jomegat (talk) 20:54, 13 March 2008 (UTC)

title: Wikijunior talk:Animal Alphabet/B


text:
User talk:82.83.50.16

Welcome!
Welcome to Wikibooks, a collection of open-content textbooks! You don't have to log in to read or edit articles on Wikibooks, but creating an account is quick, free and non-intrusive, requires no personal information, and gives you many benefits, including:
 * The use of a username of your choice
 * The ability to view all your contributions via a "My contributions" link
 * Your own user page
 * Your own talk page which, if you choose, also allows users to send you messages without knowing your e-mail address
 * The use of your own personal watchlist to which you can add articles that interest you
 * The ability to rename pages.
 * The ability to upload images
 * The ability to customize the appearance and behavior of the website
 * The eligibility to become an administrator
 * The right to be heard in votes and elections
 * Your IP address will no longer be visible to other users.

We hope that you choose to become a Wikibookian and create an account. Feel free to ask me any questions you may have on my talk page. By the way, make sure to sign your posts and comments with four tildes (~~~~), which will let others know who left it.

Νεοπτόλεμος ( talk | email | contribs ) 21:07, 13 March 2008 (UTC)

title: User talk:82.83.50.16


text: User talk:67.176.243.104

title: User talk:67.176.243.104


text:
User talk:Bmolitor

Welcome, !

Come introduce yourself at the new users page. If you have any questions, you can ask there or contact me personally. Νεοπτόλεμος ( talk | email | contribs ) 21:53, 13 March 2008 (UTC)

title: User talk:Bmolitor


text: User talk:70.247.38.60

title: User talk:70.247.38.60


text: User talk:74.46.55.206

title: User talk:74.46.55.206


text: User talk:99.244.74.110

title: User talk:99.244.74.110


text: User talk:76.219.180.143

title: User talk:76.219.180.143


text: User talk:67.84.100.128

title: User talk:67.84.100.128


text:
User talk:82.1.15.193

Join Us!
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title: User talk:82.1.15.193


text:
Ancient History/Human Evolution

<<Return to Ancient History table of contents

title: Ancient History/Human Evolution


text:
Ancient History/Americas

The Americas

 * (wp) Olmecs
 * (wp) Chavin cult
 * (wp) Teotihuacan
 * (wp) Mayan empire
 * (wp) Origins
 * (wp) Decline of the Maya
 * (wp) Spanish conquest of the Mayas
 * (wp) Mochica
 * (wp) Ancient Cuba
 * (wp) Aztec Empire
 * (wp) Origins of the Aztec
 * (wp) The Aztecs arrive in the Valley of Mexico
 * (wp) Rise of the Aztecs
 * (wp) Aztec Triple Alliance
 * (wp) Tlacaelel and Moctezuma I
 * (wp) Tlacaelel
 * (wp) Reform of the Aztec religion
 * (wp) The height of the Empire
 * (wp) Fall of the Aztec Empire
 * (wp) The Conquest of Mesoamerica
 * (wp) The fate of the Aztec empire under Spanish rule
 * (wp) The impact of epidemics on the Aztec Empire
 * (wp) Great leaders
 * (wp) Incan Empire
 * (wp) Inca mythology
 * (wp) Emergence and expansion
 * (wp) Spanish conquest and Vilcabamba
 * (wp) After the Spanish conquest
 * (wp) Toltec Empire
 * (wp) Sacking of Teotihuacan (ca. 750).
 * (wp) The Cult of Quetzalcoatl

Also be sure to read The History of the Native Peoples of the Americas.

title: Ancient History/Americas


text:
Ancient History/Africa

Africa

 * (wp) Nubia
 * (wp) Kush
 * (wp) Ethiopia
 * (wp) Aksum
 * (wp) Bantu
 * (wp) Carthage

title: Ancient History/Africa


text:
C++ Programming/Code/Standard C Library/Functions/strcmp

strcmp
The function strcmp compares str1 and str2, then returns:

For example:

Note that if str1 or str2 are missing a null-termination character, then strcmp may not produce valid results. For a similar (and safer) function that includes explicit bounds checking, see strncmp.

 * Related topics: memcmp - strcat - strchr - strcoll - strcpy - strlen - strncmp - strxfrm


text:
C++ Programming/Code/Standard C Library/Functions/strncmp

strncmp
The strncmp function compares at most count characters of str1 and str2. The return value is as follows:

If there are less than count characters in either string, then the comparison will stop after the first null termination is encountered.

 * Related topics: strchr - strcmp - strcpy - strlen - strncat - strncpy


text: User talk:67.36.188.86

title: User talk:67.36.188.86


text:
User:Staka

— — — — — — — — — — — — — — — W ELCOME T O S TAKA'S U SERPAGE — — — — — — — — — — — — — — —

Advanced Functions, Calculus, and Vectors

 * Calculus/Functions
 * Trigonometry
 * Calculus

Grade 12 Chemistry

 * Organic Chemistry

title: User:Staka


text:
Beekeeping/Spring Management

About March or April (depending on your location and the weather), you can begin to work your hives again. Make a habit of noticing the nectar sources in your area and keep an eye out for one of those glorious spring days when the sun is shining and the temperature is 55F or more. If you've never opened a hive before check out the Opening a Hive for the First Time page.

Early Spring

 * Scrape bottom board of dead bees & other junk
 * Replace entrance reducer (this will help weaker hives protect their limited honey stores)
 * Check for evidence of laying queen
 * Check for Capped Honey. If you find none, feed the bees sugar syrup using a feeder immediately.  With no honey flow and brood being raised, a hive will consume 10 pounds of syrup per week.
 * Check for pollen, the protein source needed for rearing brood.

title: Beekeeping/Spring Management