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Cookbook:English Breakfast

| United Kingdom | Breakfast

The traditional English breakfast is ubiquitous the world over. Cafés and hotels all around the world offer a version, often far removed from what might be considered conventional.

The English breakfast as it is known today is based, like so many British traditions, on what became popular in the Victorian era. Victorian home economist Isabella Beeton gives the following advice in The Book of Household Management (1861) about breakfast:

The following list of hot dishes may perhaps assist our readers in knowing what to provide for the comfortable meal called breakfast. Broiled fish, such as mackerel, whiting, herrings, dried haddocks, &c.; mutton chops and rump-steaks, broiled sheep’s kidneys, kidneys à la maître d’hôtel, sausages, plain rashers of bacon, bacon and poached eggs, ham and poached eggs, omelets, plain boiled eggs, oeufs-au-plat, poached eggs on toast, muffins, toast, marmalade, butter, &c. &c.

The key components of a modern English breakfast include bacon, sausages, fried or poached eggs, sliced fried red tomatoes, baked beans (in cans), fresh sautéed mushrooms, fried or roast potatoes, fried bread, and black pudding. It may often include stewed prunes, buttered toast, often spread with orange marmalade, tea, and/or orange juice.

The English breakfast frequently suffers from being prepared badly and with poor quality ingredients. Cooked well, with high quality ingredients, it can be a delicious start to the day. Preparing an English breakfast is quite easy; it is basically a matter of starting off cooking the items that take the longest to cook, and moving through to the things that take the least time so that it is all ready at the same time. It is made even easier by the fact that most of the ingredients can be kept warm for a while once cooked without spoiling; this fact allows for the common way of serving English breakfasts as a kind of buffet where diners can help themselves from warm serving plates.

Ingredients

 * 4 rashers of bacon (smoked bacon without too much fat is best, e.g. smoked back bacon)
 * 4 eggs
 * 4 English-style pork sausages
 * 4 medium-sized tomatoes, halved around the equator
 * 400 g mushrooms, sliced
 * 4–8 slices of bread (traditionally white)
 * 1 tin baked beans (optional)

Method 1
This method emphasizes broiling and poaching rather than frying.

 * 1) Heat a broiler to medium heat, and cook the sausages under it, turning frequently. They should take about 10–15 minutes total to cook.
 * 2) Cover the base of a frying pan with about 1cm of water, and heat on a high heat until boiling. When it is boiling, carefully break the eggs into it. If you have cooking rings, you can put these into the water first and then break the eggs into the rings, to prevent the eggs from spreading too much, although really fresh eggs should stay together anyway. Once the eggs are in the pan, wait a few moments for the water to heat up again, then turn the heat down to a very very gently simmer. To ensure the tops of the eggs are cooked, spoon water from around the edge of the pan over the top of the eggs a few times during cooking. When cooked, the egg white should be soft but cooked through and the yolk still runny. They should take about 8–10 minutes to cook.
 * 3) Put the halved tomatoes under the broiler with the sausages. They should take about 6 minutes to cook.
 * 4) If using, put the baked beans into a saucepan and heat through over a medium heat. They should take about 5 minutes to heat through.
 * 5) Heat up a very small amount of oil in a pan, and fry the mushrooms until they are soft. They should take about 4 minutes to cook.
 * 6) Put the bacon under the grill along with the sausages and tomatoes. Cook on one side for about 2 minutes, then turn once and repeat. Cook longer if crispier bacon is preferred. This should take about 4 minutes to cook.
 * 7) Whilst cooking the bacon, toast the bread until golden.
 * 8) Serve the eggs, bacon, mushrooms, sausage, tomato and beans onto piping hot plates, with the toast on a separate plate or toast rack. Serve with butter and jam for the toast, and hot tea with milk.

Method 2
This method is more in keeping with the spirit of the dish.

 * 1) Start toasting the bread before cooking the rest of the food. Assuming 2 slices per person, you should have enough by the time you finish the fried food. Be sure to butter them heavily with real butter rather than low-fat spread. Place 4 plates on the bottom shelf of an oven, and one on the top. Set the oven to its lowest heat.
 * 2) Melt some lard in a large frying pan (enough to make a layer of fat around 1 cm deep) and brown the sausage in it over a high heat. Lower heat and cook the sausage for around 4 minutes, and leave it in the pan. A lot of fat will leak from the sausages. Add the bacon (2 strips per person rather than 1) and cook to taste, flipping regularly (2–3 minutes for pink, 4–6 for a darker red bacon with crispy fat). The bacon will also release a lot of fat. Transfer the bacon to the warmed dish in the top of the oven. Leave the sausage in the pan.
 * 3) Add the mushrooms and tomatoes to the pan. Add the tin of baked beans to a small pot and heat on a separate burner. After 2–4 minutes, transfer the mushrooms to the oven with the bacon. Transfer the tomato then too, or leave it a little longer depending on taste.
 * 4) The sausages should now be dark brown, push them to the side of the pan and break an egg into the fat. Using a spatula, push hot fat over the yolk until it begins to bubble but is still liquid. This should take about 1 minute or so in a hot pan. Set out the 4 warmed plates beforehand and add an egg to each. When done, add the sausage, bacon, and mushrooms. Add the beans last. Serve with the buttered toast on a separate plate.
 * 5) If you are using black pudding, add it to the fat with the bacon and remove it before the eggs.
 * 6) If you desire a fried slice, add a slice of bread (whole or cut diagonally, in half or quarters) and allow it to absorb some of the leftover fat and lightly fry, then flip over and repeat. Alternatively, you can just fry some bread in vegetable oil in a separate pan but it doesn't have the same flavour as bread fried in the leftover fat from cooking a full breakfast in lard. If a whole slice is used it is preferable to place the fried egg on top, so the yolk runs into the bread and can easily be absorbed by the fried slice.

Notes, tips, and variations

 * You can increase the number of eggs per person if desired.
 * If you can't cope with preparing everything all at once (or don't have enough pans / rings), it is possible to keep all of the items warm in a preheated oven, so you can just cook each item in turn and keep it warm until needed. Try not to keep the eggs warm for too long before serving though, as the yolks may harden.

title: Cookbook:English Breakfast


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User talk:TurretTower

Page moves
The odd-page moves are vandalism. If you find any more such moves, you can report it at Vandalism in progress. --Kernigh 17:49, 15 April 2006 (UTC)

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

title: User talk:TurretTower


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User talk:Maathanki06

Maththanai
Is this a new Wikibook? So far it looks like an encyclopedia-article stub. Did you mean to submit it to our sister project Wikipedia? --Kernigh 18:14, 15 April 2006 (UTC)

title: User talk:Maathanki06


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User talk:Glennherrin~enwikibooks

Glenn Herrin
Is this a new Wikibook? So far it looks like an encyclopedia-article stub. Did you mean to submit it to our sister project Wikipedia? --Kernigh 18:14, 15 April 2006 (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 Glennherrin. To make sure that both of you can use all Wikimedia projects in future, we have reserved the name Glennherrin~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 23:14, 17 March 2015 (UTC)

Renamed
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title: User talk:Glennherrin~enwikibooks


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Bicycles/What style

When you walk into a bike shop you see a huge range of different styles of bicycles. There may be bikes with enormous suspension systems, little things with ribbons sticking out, bikes that are light with very thin wheels, and big monsters you think King Kong couldn't lift. There are several main types of bicycles you'll see in your local bike shop--upright bicycles, mountain bikes, road bikes and kids bikes.

Upright bicycles or city bikes have wide saddles and swept handlebars curved towards the rider, and are suitable for transportation or utility cycling. They are particularly common in the Netherlands.

Mountain bikes are usually the bigger bikes with wider but smaller diameter wheels. As other bikes they come in many varieties. Cross-country mountain bikes are the lightest weight modern mountain bikes, with only front shocks or with low travel full suspension; the intended use being riding long distances over unpaved paths through medium terrain, like hiking on a bicycle. For more aggressive mountain bikers, all-mountain, freeride, or downhill mountain bikes exist. They are for going down steep slopes at high speeds, over big drops. They are extremely strong, but heavy, and not designed to be pedaled for much distance. In many places they are taken up ski lifts in the summer, or driven up in a automobile, and only ridden down hill.

Road bikes are designed for road riding as a sport. They are suited for speed and efficiency. For example, the thin tires cut down on rolling resistance and the ultra light frames allow riders to reach some amazing speeds with the least effort.

You might see cyclocross bikes, which are similar to road bikes in geometry, but are built to take larger tires and be ridden off-road. Often, there are separate brake levers on the tops of the road handlebars.

There are many types of bicycle available. Choosing the bicycle that fits your needs is an important first step to enjoying your cycling experience. This chapter aims to weigh the pros and cons of some cycles.

Transport or utility biking
Pros: Cons:
 * The most comfortable after recumbent.
 * Suitable for sore backs or riders with back trouble.
 * Good for maintaining upright posture for all riders in good health.
 * Appropriate for roads in cities and towns.
 * Superior rider visibility.
 * Appeals to women with wide saddles and step-through frames.
 * Good for transporting luggage.
 * Accessories such as front baskets, bike racks, chain guards and kickstands common.
 * Bad off-road capability.
 * Slower than road bicycles.
 * Less portable - no quick release wheel.
 * Kerbs are difficult to mount in urban environments.
 * Unusual for male bicycle riders in certain countries.
 * Less popular and therefore less available in some countries.

Road biking
Pros:
 * Roads are easily accessible.
 * Speeds can reach well in excess of 40KPH.
 * Can be made easy or hard (if you ride long or fast or take hills).
 * Can be very enjoyable and exhilarating.
 * Burns many calories and increases physical fitness.

Cons:
 * Can be dull, rigorous and sweaty.
 * Traffic requires being aware of situations and using safe skills.
 * Fast riding and descending require skill.
 * Entry-level road bikes tend to cost more than entry-level mountain or "hybrid" bikes.
 * Crashes at high-speed are very dangerous.

Cross-country Mountain Biking
Pros:
 * Very challenging
 * Very good exercise.
 * Scenery is usually better than road biking.
 * Facilities and Trails accessible.

Cons:
 * Hard.
 * Can be tiring.
 * Smooth ride is a joke
 * Facilities not as easily accessible as road biking.
 * Also dangerous!

This type of riding is for die-hard individuals, and people who like hiking.

Freeride Mountain Biking
Pros:
 * Increasingly popular.
 * If you like skiing...
 * Fast.
 * Going off jumps is an exhilarating experience (once you get used to it).
 * Fairly challenging.
 * Truckload of fun.
 * Safe if rider is wearing body armor.
 * You can do big tricks in this type of riding.

Cons:
 * Dangerous if rider is not wearing body armor.
 * Scary at first.
 * Hard to access.
 * Not good exercise.
 * Expensive.

In slopestyle, riders can perform tricks. For daredevils with lots of money and health insurance.

Recumbent Bikes
Pros:
 * Comfortable.
 * The fastest of all bicycle styles.
 * Excellent exercise.
 * Can ride longer distances in comfort.
 * With proper gearing, can climb hills easily.

Cons:
 * Not ideal for riding in urban conditions due to low riding position. Cars may have trouble seeing you.
 * Recumbent bicycles tend to be more expensive because they are not mass produced.
 * Recumbents tend to be harder to find for test rides.
 * More skill needed to balance (unless you're riding a recumbent trike!).
 * Not as well understood by bike mechanics and shops.
 * Climbing hills can be more difficult if one is used to standing up off the pedals to climb in an improperly high gear on a diamond frame bicycle, although extra leverage can be gained by pushing against the back of the seat. As noted in advantages, this is not an issue with proper gearing.

title: Bicycles/What style


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How to use a Motorola DVR/Connections

Need to add info and/or pictures on connecting the DVR to a home entertainment/TV/whatever system.

DVR Connector Descriptions
For photo illustrations of the various DCT models' connections panels, please refer to the "Identify" module, in this Wikibook.

DCT-34xx
The 34xx series has no front panel connections.

Rear Panel (From left to right):
 * 1 Coaxial RF connector (CABLE IN for signal from the cable company)
 * 1 Coaxial RF connector (RF OUT for a TV or other device)
 * 1 IR repeater port (1/8 inch socket)
 * 1 S-Video OUT
 * 1 Coaxial SPDIF OUT (digital audio, orange RCA)
 * 1 Optical SPDIF OUT (digital audio)
 * 1 Composite video OUT (yellow RCA)
 * 1 pair Audio OUT (Left [white] & Right [red] RCA)
 * 1 triplet Component video OUT (Y [green], Pb [blue], Pr [red] RCA)
 * 1 HDMI
 * 1 Ethernet
 * 1 USB
 * 1 SATA
 * 2 IEEE 1394 (also known as Firewire or i.Link)
 * 1 Power outlet (to power another device. It may or may not be powered on and off with the DVR.)
 * 1 Power IN (power cord is removable)

NOTE: Your cable company controls which ports are active. Typically, the USB, SATA and Ethernet ports are disabled. The USB port may supply power for devices like a fan or light.

DCT-64xx Phase III
Front Panel:
 * 1 Composite video IN (yellow RCA)
 * 1 pair Audio IN (Left (white) & Right [red] RCA)
 * 1 USB
 * 1 SmartCard

NOTE: Most cable companies disable the front panel connections. The USB port may still supply power to run a fan or light.

Rear Panel (From left to right):
 * 1 Coaxial RF connector (CABLE IN for the signal from the cable company)
 * 1 Coaxial RF connector ((Some Models Only)RF OUT for a TV or other device)
 * 1 IR repeater port (1/8 inch socket)
 * 1 S-Video OUT
 * 1 Optical SPDIF OUT (digital audio)
 * 1 pair Audio IN (Left [white] & Right [red] RCA)
 * 1 pair Audio OUT (Left [white] & Right [red] RCA)
 * 1 Coaxial SPDIF OUT (digital audio, orange RCA)
 * 1 triplet Component video OUT (Y [green], Pb [blue], Pr [red] RCA)
 * 1 Composite video IN (yellow RCA)
 * 1 Composite video OUT (yellow RCA)
 * 1 HDMI
 * 1 USB
 * 1 SATA
 * 2 IEEE 1394 (also known as Firewire or i.Link)
 * 1 Ethernet
 * 1 Power outlet (to power another device. It may or may not be powered on and off with the DVR.)
 * 1 Power IN (the power cord is removable)

NOTE: Your cable company controls which ports are active. Typically, the USB, SATA, composite video IN and Ethernet ports are disabled. The Audio IN ports will pass audio through to the audio out when the DVR is turned off. The USB port may supply power for devices like a fan or light.

DCT-64xx Phase II versions 1 & 2
Version 1 Phase II's have no coaxial RF output and only one USB port on the back.

Front Panel:
 * 1 Composite video IN (yellow RCA)
 * 1 pair Audio IN (Left (white) & Right [red] RCA)
 * 1 USB
 * 1 SmartCard

NOTE: Most cable companies disable the front panel connections. The USB port may still supply power to run a fan, a light, iPods or even PS3 controllers. (Personal note: My Gen5.5 30G iPod appears to recognize the connection by turning on, but will not actually charge the battery when connected to my 6412 Phase II.)

Rear Panel (from left to right):
 * 1 Coaxial RF connector (CABLE IN for the signal from the cable company)
 * 1 Coaxial RF connector (Version 2 only, RF OUT for a TV or other device)
 * 1 IR repeater port (1/8 inch socket)
 * 1 Ethernet
 * 1 USB (Version 2 has 2 USB ports)
 * 1 DVI
 * 1 pair Audio IN (Left (white) & Right [red] RCA)
 * 1 pair Audio OUT (Left (white) & Right [red] RCA)
 * 1 Coaxial SPDIF OUT (digital audio, orange RCA)
 * 1 triplet Component video OUT (Y [green], Pb [blue], Pr [red] RCA)
 * 1 Composite video IN (yellow RCA)
 * 1 Composite video OUT (yellow RCA)
 * 1 S-Video OUT
 * 1 Optical SPDIF OUT (digital audio)
 * 2 IEEE 1394 (also known as Firewire or i.Link)
 * 1 Power outlet (to power another device. It may or may not be powered on and off with the DVR.)
 * 1 Power IN (power cord is removable)

NOTE: Your cable company controls which ports are active. Typically, the USB, composite video IN and Ethernet ports are disabled. The Audio IN ports will pass audio through to Audio OUT when the DVR is turned off. The USB port may supply power for devices like a fan or light.

DCT-64xx Phase I
Need information about Phase I DVRs.

Connection samples
Below are a few basic connection ideas for common situations.

SD TV with no A/V inputs
You either must use a DCT-64xx Phase III or DCT-34xx, or purchase an RF Modulator.

 * 1) Connect coaxial cable from cable company to DVR's CABLE IN connector
 * 2) Connect coaxial cable from the DVR's RF OUT connector to your TV (alternatively, you can connect it to a VCR or DVD recorder's RF input, and connect it's RF output to your TV.)
 * 3) If your DVR does not have an RF out connection, purchase an RF Modulator. Connect the DVR's Composite video OUT (yellow RCA) jack to the modulator. Connect the DVR's audio OUT (Left [white] & Right [red] RCA) jacks to the modulator.
 * 4) Tune your TV to channel 3 (or sometimes channel 4)
 * 5) Refer to the Setup page and change the YPbPr Output setting to 480i.

SD TV with A/V inputs

 * 1) Connect coaxial cable from cable company to the DVR's CABLE IN connector
 * 2) (optional) Connect coaxial cable from the DVR's RF OUT connector to your TV (alternatively, you can connect it to a VCR or DVD recorder's RF input, and connect it's RF output to your TV.)
 * 3) Connect the DVR's audio OUT (Left [white] & Right [red] RCA) jacks to your TV's Audio IN jacks.
 * 4) Determine the highest quality connection your TV supports. From highest to lowest, these will be Component, S-Video, then Composite. (If you have a rare standard definition TV that has HDMI or DVI ports, those should be considered highest quality.)
 * 5) Make your video connection:
 * 6) Component: Use 3 RCA cables, typically color coded green (Y), blue (Pb), and red (Pr).
 * 7) S-Video: Use cable with large round connector that has 4 pins and a plastic post inside it.
 * 8) Composite: Use an RCA cable, typically color coded yellow.
 * 9) Tune your TV to the video input you made your connections to.
 * 10) Refer to the Setup page and change the YPbPr Output setting to 480i.

title: How to use a Motorola DVR/Connections


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How to use a Motorola DVR/Setup

Setting video display options
The DVR has several options to configure the video output format for your TV or display. This includes HD modes, SD mode, screen format (4:3 or 16:9), and closed captioning. Some newer models with the latest firmware also have options to fine tune DVI or HDMI settings.

Accessing the user settings menu
To access the video options, you need to go to USER SETTINGS
 * 1) Turn the DVR off.
 * 2) Press the Menu button on the remote or the front of the DVR.

Accessing the user settings menu: Verizon FiOS TV with IMG v2.0
Subscribers to Verizon's FiOS TV that have the IMG v2.0 have a slightly different method to enter USER SETTINGS. Perform the following steps quickly (pauses between button presses may prevent the menu from appearing):
 * 1) Press the power button to turn the DVR off. Be prepared to quickly press the next 2 buttons.
 * 2) Immediately press and release the OK button on the remote (or the Select button on the front of the DVR)
 * 3) Immediately press and release the Menu button on the remote or the front of the DVR.
 * 4) If your current aspect ratio does not display (16:9, 4:3L, or 4:3P) you may have waited too long between button presses. Turn the DVR on and try again.

Alternately, FiOS TV subscribers with IMG 2.0 may access the user settings menu during the DVR's boot sequence. Note that with this approach, the menu will go away when the DVR finishes booting (in a minute or two):
 * 1) Unplug the DVR for 30+ seconds.
 * 2) Plug in the DVR
 * 3) Press the Menu button on the front of the DVR when --:-- shows on the front of the DVR.
 * 4) If your current aspect ratio does not display (16:9, 4:3L, or 4:3P) you may not have had the DVR powered off long enough. Repeat the steps above but leave the DVR unplugged longer.

Navigating in the user settings menu
While in the menu, the up or down arrows move between options. The left and right arrows will change the selected option.

To exit, press the Power key on the remote or the front of the DVR.

If you are unable to see the video on your display, most of the options will also display on the front panel of the DVR.

If you tune into a SD channel before turning off the DVR, the user settings menu will display in standard 480i

TV Type
TV TYPE is where you specify the screen format. This only appears to affect how HD material is displayed when downconverted to 480i (SD) or 480p (ED).

The options are:

HDMI/YPbPr Output
HDMI/YPbPr OUTPUT sets the HD format used by the component, DVI, or HDMI outputs. The RF, composite, and S-Video outputs will ALWAYS be 480i.

The DVR can only output one HD format. For example, if you set it to 1080i, all HD will be output as 1080i. Any source that is 720p or 480p will be converted to 1080i. This is only done when on playback or viewing live video. Recordings are ALWAYS saved in their native format.

WARNING: If HDMI/YPbPr OUTPUT is set to anything other than 480i, and you are watching HD material, you will NOT be able to see the on-screen menus on the RF, composite, or S-Video outputs.

WARNING: As you scroll through the options, the output will change to that format. If you are using the RF, composite, or S-Video output, the video may go blank until you go back to 480i.

The options are:

Which HDMI/YPbPr Output Setting Should I Use?
If your display is not HD capable, then set HDMI/YPbPr OUTPUT to 480i. This will guarantee you can always see the menus. Set the TV Type selection to match your display aspect ratio and letterboxing preferences when viewing HD material (which will be downconverted for your TV).

If your display is HD capable, there is no hard and fast rule. You need to check the owners manual, or information on the back panel of the TV to find out what resolutions it accepts.

If it's an EDTV, then a setting of 480P will probably work best.

If it's CRT-based (direct-view or projection), then 1080i may be the best option, as most display 1080i natively.

If it's a fixed resolution panel such as Plasma, LCD, DLP, LCoS, SXRD or similar, it depends on its vertical resolution. That is typically the second number listed: 1920 x 1080 would have a vertical resolution of 1080 lines. If that number matches one of the HDMI/YPbPr OUTPUT options, try that first. If it's an oddball number like 768 or 786 or 1024, then it's a matter of trial-and-error to find which format you like and that works best with your display.

4:3 OVERRIDE
4:3 OVERRIDE tells the DVR how to output SD programming. This option is disabled if HDMI/YPbPr OUTPUT is set to 480i.

The options are:

You should try the 480I (no conversion) setting first. Most newer displays do a better job handling SD upconversion than the Motorola. Also, most widescreen displays offer more "zoom" options in 480I for material that is already letterboxed, to fill the widescreen. If you choose one of the other settings for 4:3 OVERRIDE, these "zoom" setting may not be available.

NOTE: On DCX models when "Native" mode is chosen under HDMI/YPbPR OUTPUT, the 4:3 OVERRIDE setting is greyed out and has no effect.

Additional HDMI Settings
The 641x-PIII and 341x include an HDMI output instead of a DVI output. As of Firmware 16.20, a new option, "ADDITIONAL HDMI SETTINGS >>>" was added to the menu. Highlighting it and pressing OK/Select will switch to a second screen.

You can arrow down to each option and press the OK/Select to change it.

The options are:

This is a draft in-progress for updates to the Motorola DVR page.

Closed Caption
The way that closed captioning works depends on the type of cable used to connect the DVR to your TV.

Closed Caption: Coaxial, S-Video, or RCA video
Use your TV's built-in closed caption decoding to display closed captions when you connect the DVR to the TV with any of the following:

 * Coaxial RF OUT: The typical screw-on cable connector.
 * Composite video: The yellow RCA jack.
 * S-Video

Your TV may have a closed caption button on the remote (often labeled "CC"), or else you may need to use your TV's on-screen menu system to enable decoding of closed captions.

Closed Caption: HDMI, Component, etc
You must use the USER SETTINGS menu on the DVR if you connect with any other cable type, including HDMI and component (YPbPr). You can not use your TV's closed caption features because these other connections can not carry the closed caption signal. Instead, you must tell the DVR to decode closed captions, and then overlay them on the video sent to the TV.

Unfortunately, it is very inconvenient to switch between displaying and hiding closed captions. You must use the USER SETTINGS menu which requires you to power-off your DVR. After accessing the menu (see above), move down to the CLOSED CAPTION entry then change DISABLED to ENABLED. When you power on the DVR again the next time, captions will always be displayed.

There are some other caption settings when ENABLED which are mostly self explanatory. For ANALOG, CC1 is the standard closed captioning channel. CC2, or CC3 is often used for Spanish captioning.

For more details on the limitations of HDMI and component connections, see the HDTV interoperability issues section of the Wikipedia page on closed captions.

Subtitle Settings
As of Firmware 16.20, the user menu has a SUBTITLE SETTINGS >>> option at the top of the display. Highlighting it and pressing OK/select will switch to a second screen.

The second screen offers options for STATUS (ON or OFF), and LANGUAGE (ENG [English], FRE [French], SPA [Spanish], and POR [Portuguese].)

To exit the screen, highlight the RETURN TO MAIN MENU >>> option at the bottom.

It's unknown what the subtitle settings are used for.

Restore All Defaults
RESTORE ALL DEFAULTS will reset all options to common defaults.

This will typically be:

title: How to use a Motorola DVR/Setup


text:
College Survival Guide/Choosing Supplies

Academic Supplies
What you carry every day to class has a huge impact on your college experience.

Bag
A high quality Backpack or Messenger Bag is key for protecting your stuff from the elements. Get one with lots of pockets.

Stationery
You will want a 5 subject notebook or a three ring organizer and loadable paper. If you take notes on a laptop or tablet, bring a smaller notebook for emergency paper. In class it is not uncommon for some professors to issue impromptu assignments. Without paper you'll be dead in the water. Furthermore, should you run out of battery, you will still be able to take notes.

Your writing utensils are very important. They should be comfortable in your hand and suit your writing style. You will want a good quality black ink ballpoint pen and quality mechanical pencils as your main writing utensils. It helps to bring a red and blue pen for marking up work, though some prefer an all in one multicolor pen. Highlighters and post it notes are essential tools when annotating handouts, and your own books.

Calculators
Each professor or department will have their own opinion or policy on calculator use. Some let anything go. Some will require a specific brand of calculator. Some classes, especially remedial ones, will put restrictions on how good the calculator can be, and might even prohibit any calculator. These restrictions most commonly prohibit calculators with Computer Algebra Systems (CAS), Programmability, or Graphing Capabilities built in. Get the calculator that is recommended by your professor.

For general use a scientific calculator or a graphing calculator is a good thing to have on hand for when you need to do unexpected calculations.

To verify a calculator is working properly and is good enough for general use, try calculating $\sqrt{2}$⋅$\sqrt{2}$. If it's answer is anything other than 2, you should reconsider relying on that calculator.

Business students ought to consider getting a financial calculator. These calculators have common functions used in Business coursework built in.

Flash Drives
Sometimes you may find yourself in situations where you lack the time to upload a large file to the cloud for a quick transfer, or find yourself on an offline computer with important documents. A flash drive is invaluable in these situations. Get one that can attach to a lanyard or keychain so you don't loose it.

Computers

Some programs in your school may have a computer requirement, requiring that you own a computer. Some programs will go a step farther and require minimum specifications your computer must meet. Some programs go even farther and require a computer from a specific manufacturer, or even a specific model of computer. In these cases, get a computer that meets your schools requirements. Most Professors look dimly on students who disrupt class by not being properly prepared.

If your school does not have a computer requirement, you may be able to save money by relying on computer labs operated by the university.

Laptop or Desktop or Tablet
Laptops can be a convenience, but sometimes they aren't a needed item. If you get easily distracted in class, forcing yourself to leave your computer at home by getting a desktop can be a smart move, assuming your professor doesn't require a laptop for in class work. Desktops are often cheaper then an equivalent laptop, and offer several advantages, such as larger screens, more ergonomic keyboard options, and other perks. Some laptops support docking, which allow them to act like desktops. Furthermore, the widespread use of laptops on campuses have lead many professors to unofficially expect students to have one.

For a student looking to take notes in class and very little else, they would do fine with a simple paper notebook or a tablet computer. In this case, a student should still have access to a fully featured computer, as professors may assign work requiring a computer without outlining an official computer requirement in their syllabus.

Digital Divide
Sometimes computers fail, or a student can not afford a computer. In these cases a college may have solutions. Some colleges offer laptop loan programs, which allow students to borrow a computer for a semester, often for free if the computer is returned undamaged. Many colleges still maintain computer labs, which offer an office like environment for conducting scholarly or professional work.

If you have a computer, but it is unable to run heavy applications such as those used for engineering or complex 3D rendering, you may consider a cloud desktop service. These usually charge by the hour or month, and allow you to use a server to run your software and stream a desktop to your device.

Portable Storage
Sometimes lab computers are configured in a way that allows the running of portable applications. These are special applications designed to run from a flash drive or cloud storage without traditional installation.

Learn to use the network resources offered by your college such as cloud storage solutions or other resources.

Open Source Software
When selecting software, you should consider using Open Source Software when possible. Open Source software is free as in freedom, and often free as in beer. Additionally Open Source software can often be used on Windows, Linux, and Macintosh computers.

Common Applications
Some commons open source applications useful for students include.
 * LibreOffice - Office suite with general compatibility with Microsoft Office including word processor, spreadsheet, presentation and drawing.
 * Zotero citation reference management
 * Xournal++ helps with note-taking like Microsoft OneNote supporting handwriting input.
 * Freeplane is mind mapping and knowledge management.
 * Mozilla Firefox - Web Browser
 * uBlock Origin - Browser extension used to block undesired content.
 * HTTPS Everywhere - Browser extension that helps with general online security.
 * Mozilla Thunderbird - Email client.
 * VLC media player - Good for viewing most media formats.
 * Bitwarden - Password Manager.
 * Calibre - Ebook manager.
 * GnuCash - Personal finance manager.

Applications more useful for specific majors include

Art & Humanities

 * Blender - 3D art suite.
 * Krita - 2D digital drawing painting and 2D animation.
 * Inkscape - Vector graphics editor.
 * GNU Image Manipulation Program - Raster image editor.
 * Synfig - 2D animation application.
 * Darktable - Non-destructive photo editor
 * Scribus - Desktop publishing application.
 * Godot - 2D & 3D Game engine.

STEM

 * PuTTY - Terminal application.
 * FlightGear - Flight Simulator
 * FreeCAD - 3D Computer Aided Design application.
 * LibreCAD - 2D Computer Aided Design application.
 * KiCad - Electronic design automation
 * R - Statistical programming environment
 * QGIS - Geographic Information System Software.

Furniture & Appliances
When getting supplies for your dorm room, it's important to find out what's already there. Having two microwaves is rarely useful. Look up the dimensions of your room - Even a minifridge may not fit in a small room for example.

You certainly don't need every appliance on this list. Indeed, if you are living on campus a number of these items may in fact be prohibited, though what is and isn't allowed depends on your individual college. Most items in the Cooking list are either included in a dormitory kitchen or banned outright, typically for fire safety. If you rent a private dwelling off campus, you will have more freedom in what you may bring, with the added responsibility of those items.

Cooking

 * Electric Kettle or Coffee Maker. Tea or Coffee prepared by yourself is often much cheaper.
 * Microwave, Toaster, or Toaster Oven for quick snacks. Consider an oven if living off campus.
 * Mini-fridge. Consider a full size fridge if living off campus.
 * Insulated Lunchbox, Bottle. Being able to prepare your own meals saves serious cash over eating out.
 * Travel Silverware.
 * Dish Soap, Rags or Paper Towels, Sponge.

Comfort

 * Box Fan. Even if your room has air conditioning, there's a good chance it's centralized and won't perform to your standards.
 * Dehumidifier. Reducing the humidity of your room can make it feel cooler.
 * Extra blankets can be used to keep warm on cooler nights.

Security
Create a spreadsheet listing all items you are bringing with you of nontrivial cost, along with short descriptions of unique markings or serial numbers. Save it in an online account.

 * Safe. A small safe or locked box for sensitive documents, medication, laptops, etc will help deter theft. Generally there are no good ways to mount a safe in a dorm or apartment, so consider investing in a sturdy cable to tie it to permanent room fixtures or large furniture.
 * K-Locks for stationary electronics. They won't stop determined thieves, but they will stop people from just walking off with your stuff.
 * Permanent Markers. Write property of "YOUR NAME" on expensive items in hard to find areas, so you can prove your ownership if needed.
 * Bicycle license. Your city may allow you to register your bike with local police. Having your bike serial number on record makes it harder to resell.

Clothes
You'll want good, durable clothes for the environment you're in. If you're studying in Florida, leave the heavy winter coat at home.

Bring at least one set of formalwear. Doesn't have to be expensive, you can typically find cheap suits at thrift stores.

Good shoes that fit you well are paramount if you walk to class. Bad shoes let water in, and give you blisters.

A swimsuit is useful to bring if your gym has a pool, hot tub, or lazy river. It's also good if you're near an ocean or a large lake.

If you have clothes with the logo of rival schools on it, leave them behind. Get at least one piece of clothing with your school logo on it.

Groceries
Learning to eat cheap is a good way to save money during college.

There are a lot of foods that you can easily prepare with variety without access to an oven.
 * Instant Noodles (Ramen, Udon, Mee Goreng, Chow Mein)
 * Instant Soup (Tomato, Tomato Bisque, Vegetable, Minestrone)
 * Microwavable rice (Top with a variety of sauces, instant curry, etc)
 * Texas Toast (Garlic, Cheese)
 * Toast (Add Jam, Butter, or Avocado for flavor)
 * Sandwiches (Peanut Butter and Jelly, Cheese, etc)
 * Apples, Bananas, Grapes, and Olives.
 * Pizza (Leftover, Microwavable, Bites)
 * French Bread
 * Nachos (Microwave shredded cheese on chips, or buy queso dip)
 * Potatoes, Baked Potatoes, Instant Mashed Potatoes, Microwavable hashbrowns, fries.
 * Instant Pasta
 * Jerky
 * Microwave Quesadilla
 * S'mores

You can make these cheap foods more palatable with a small selection of spices and sauces. Salt, Pepper, Ketchup, Mustard, Dijon, Mayo, BBQ sauce, Hot Sauce, Sriracha Sauce, Teriyaki sauce, and Soy Sauce can put a new spin on food before you get tired of it.

Check out the Microwave Cooking cookbook for more info.

Personal Care
You'll also want some supplies for personal care. Below is a list you can tailor to your own needs.
 * Laundry detergent.
 * Laundry bag or basket (Ideally collapsable to save space)
 * Shampoo, Conditioner, and Body Wash (3 In One saves space)
 * Comb or brush
 * Basic First Aid Kit (Doesn't have to be fancy. Have some bandages, antibiotic ointment, etc.)
 * Sandals and a robe, if using communal showers.
 * Toothbrush, Toothpaste, and Floss.
 * Razors, shaving supplies
 * Earplugs and Eyemask. If there's unavoidable noise or bright light, you'll want to be sure you can get some sleep regardless.
 * Condoms. You can often get these for free at University Health centers.
 * Feminine hygiene products. You may be able to get these for free from Student Government Initiatives or a Women's center.


text:
How to use a Motorola DVR/Boot Error Codes

Boot Error Codes
If hardware or software problems occur, the DVR displays error codes on the LED display.


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Talk:Blender 3D: Noob to Pro/Build a skybox

It went through this tutorial in Blender 2.41 and my Skymap did not come out right. In .37 it works fine. I added how to touch up the final result in Photoshop at the end of the tut. ~Elysiun sn Anoncompboy

Whoa... on 5/15/2007 I accidentally deleted the top of this page (was just trying to fix 1 typo) ... it think i have it properly restored to its correct form.

Hey someone should put somewhere in there the tip that you can also use blender alone to create skybox textures for some other project. i.e. make a scene in blender and envmap it to the cube.

I managed to get an environment map. How do i use it in a blender game? Like the one in the previous tutorial?

The textures are drawn only on the outside of the skydome, not the inside where it's needed. Perhaps this article needs updating for 2.49b or 3.0. In game, the dome looks black even with sun lighting. Also textures don't display with viewport set to draw type: texture (shaded mode works). --Spudgunne (talk) 20:19, 12 October 2009 (UTC)


text:
Cookbook:Sausage Casing

Sausage casing is the outer "skin" of the sausage, sometimes made from the intestines of animals.

title: Cookbook:Sausage Casing


text:
User:Mmmooonnnsssttteeerrr

Email 10464307@uts.edu.au

Books I wrote or I'm reading

 * User:Mmmooonnnsssttteeerrr/Trigonometry

 * User:Mmmooonnnsssttteeerrr/Calculus

 * Shell Programming

 * Calculus/Vectors

 * Discrete Mathematics

 * Elementary Calculus

 * Trigonometry

 * Multivariate Calculus

 * Number Theory

 * User:Mmmooonnnsssttteeerrr/Sandbox

title: User:Mmmooonnnsssttteeerrr


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Talk:Wi-Fi/Setting up a hotspot

I have contributed a lot to this wikibook on an anonymous basis, and I would support adding this to the Wifi wikibook. The WiFi wikibook, on the other hand, appears to be a disjointed set of links and random communication and information loosely related to wireless networking that I don't think is appropriate for wikibooks. 128.82.15.5 03:22, 16 April 2006 (UTC)

 * I've redirected that one here and done some work on this one. Hope it's better now... 68.39.174.238 10:42, 27 September 2006 (UTC)

This section should stay seperate, and needs to be substantially edited and added to.

There is a large amount of arguable and circumstantial information provided, as well has an immense lack of information in many areas.

Are the basics addressed? Yes. But for the depth of information presented, it should be revised to have some corrections made, as well as more information added.

I agree that a lot of the discussion is unsubstantiated or worse. I think a lot of basic stuff is missing. The material that is present is more like a how-to guide than a real detailed treatment of the material. There is no discussion of frequency hopping, channel allocation, the relationship between US, European and other countries wireless regulation. Missing material includes 802.11a, 802.11n, pre-N and other variants plus all of the non-802.11 network variants. Nexus501 (talk) 23:47, 26 September 2009 (UTC)

title: Talk:Wi-Fi/Setting up a hotspot


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Proteomics/Protein Identification - Mass Spectrometry/Types Mass Spectrometry

This Section:

=Types of Mass Spectrometry= Previous Section: Instrumentation

AMS (Accelerator Mass Spectrometry)
In AMS (Accelerator Mass Spectrometry), a “tandem accelerator” is used to accelerate the ions at several million volts. This tandem accelerator works twice. During the first stage, negative ions are created from an ion source. These negative ions are accelerated by an electrostatic accelerator to very high kinetic energies. Then a sheet of carbon is introduced in to the instrument, to convert the negative ions into positive ions. Since these ions are now positive, they accelerate away from the center rapidly. Now a velocity selector with a combination of both electric and magnetic fields is used to allow the ions with particular mass and kinetic energy through. Finally m/z is determined by passing through a magnetic or electric sector mass analyzer.

Gas Chromatography-MS
Gas chromatography separates the components of a mixture and mass spectroscopy characterizes each of the components individually. This method is a preferred method within the proteomics community, and is known as a "golden standard" for analysis.[] In gas chromatography (GC), the mobile phase is an inert gas such as helium. Gas chromatography is a method in which molecules are separated based on volatility and bond characteristics when subjected to a carrier gas. The sample enters a vacuum chamber through an inlet and is converted into gas phase ions. The ions are sorted according to their mass to charge ratios, usually with a quadrupole or ion trap. This data is converted into representative electrical signals and finally, a mass spectrum is created.

This technique is a simple type of chromatography that is coupled to a mass spectrometer. When coupled with MS it is known as a hyphenated analytical technique due to the combination of two separately performed techniques. Dependent on the type of chromatography, buffers, and conditions, some methods of separations can be coupled with MS and some cannot. GC is a method that can normally be coupled with MS due to the samples already being in a volatile form, the form that MS can only read in. Due to the lack of buffers and salts this method does not interfere with the MS detection ability.

A great advantage to this method is that a researcher can take an organic solution, inject it into the instrument, separate the individual components, and identify each of them. Furthermore, the researcher can determine the quantities (concentrations) of each of the components.

There are some important limitations to GC-MS:

If the GC instrument does not separate the samples compounds completely or correctly, the MS feed is impure. If this occurs, background noise can appear in the mass spectrum resulting in poor resolution and poor retention times which can cause significant error in data.

Of course, the MS portion of the coupling involves a large amount of analysis from a skilled technician. Many aspects come into play, and the analyst must correlate computer calculations with system conditions. This can produce a large amount of human error within the data.

Liquid Chromatography-MS
LC-MS separates compounds chromatographically before they are introduced to the ion source and mass spectrometer by means of using liquid mobile phases which ultimately must be volatilized before entering the MS. It differs from GC-MS in that the mobile phase is liquid, usually a combination of water, organic solvents, and samples instead of gases. The method of coupling high performance liquid chromatography (HPLC) can also be performed with MS. A HPLC simply uses a smaller column that is highly chemically modified to separate on a more precise level than normal LC. Once a sample is injected it goes through a column which separates it based on charge and goes into a drying chamber where the sample is volatilized by a drying gas such as N2. The ions are then collected into a gas capillary where they are collected to be injected further in the system. When the ions proceed out of the gas capillary, the ions go through an area where collision activated dissociation occurs between a skimmer and the capillary, causing the ions to exit individually. The area where the gas capillary and the skimmer meet is the area where volatilization begins. From the capillary, the liquid ions are put through a "Taylor cone". The Taylor cone creates the effect of a fine filament of liquid that volatilizes into a gaseous form by changing its stable liquid droplets to unstable liquid droplets before changing them to gas phase ions. The samples then proceed to an inlet for the mass spectroscopy machine into a quadrupole where they are further separated by charge to mass and then moved to a detector to obtain a mass spectrum.

ICP-MS (Inductively Coupled Plasma-Mass spectrometry )
ICP-MS involves the formation of gas containing electrons, ions and neutral particles from Argon gas. The sample is atomized and ionized by this gas. In a high vacuum mass analyzer, these ionized atoms from gas are passed through cones (apertures). Based on the m/z ratio, the isotopes of the elements can be identified. The intensity of the element’s peak in the mass spectrum will be proportional to the amount of the isotope in the original sample.

IRMS (Isotope Ratio Mass Spectrometry)
Isotope ratio mass spectrometery (IRMS) is used to measure mixture of stable isotopes. It has two inlets that help in repetitive measurements with continuous supply of sample gases. This supply is sequentially switched over by a valve. This instrument has collector with conductive metal vessels that neutralizes ions, also multicollectors in some of them allowing detection of multiple isotopes. Samples that are introduced in to this instrument should be pure gases obtained from combustion or chemical trapping. An isotopic make up of a sample can be obtained by comparing the standard isotopes to the detected isotopes from the sample.

Ion Mobility Spectrometry-MS
Previously it was believed that this method could not be coupled with MS due to its non-volatile state as well as reaction of buffers, however a few groups have been experimenting with techniques and methods to couple these two performances to be able to analyze simple samples. Experiments and current tests are attempting to couple these two by using a curtain gas from the MS as a drift gas for the ion mobility to allow proper gaseous form for the MS to run. This method is believed to be a fast and cheaper alternative to the slower expensive methods of separations for those samples that do not require much resolution.

The design of the ion mobility spectrometer allows reasonably fast installation (about 1 hour), and thus the ion mobility spectrometer can be considered as an accessory of the mass spectrometer. The ion mobility spectrometer module can also be used as an independently operated device when equipped with a Faraday cup detector. The drift tube of the ion mobility spectrometer module consists of inlet, desolvation, drift, and extraction regions. The desolvation, drift and extraction regions are separated by ion gates. The inlet region has the shape of a stainless steel cup equipped with a small orifice. Ion mobility spectrometer drift gas is introduced through a curtain gas line from an original flange of the mass spectrometer. After passing through the drift tube, the drift gas serves as a curtain gas for the ion-sampling orifice of the ion mobility spectrometer before entering the ion source. Counter-flow of the drift gas improves evaporation of the solvent from the electrosprayed sample. Drift gas is pumped away from the ion source through the original exhaust orifice of the ion source. Initial characterization of the ion mobility spectrometer device includes determination of resolving power values for a selected set of test compounds, separation of a simple mixture, and comparison of the sensitivity of the electrospray ionization ion mobility spectrometry/mass spectrometry (ESI-IMS/MS) mode with that of the ESI-MS mode. (Sysoev, A 2004)

MALDI-TOF
Matrix Assisted Laser Desorption Ionisation (MALDI) (F. Hillenkamp, 1991) deals with thermolabile, non-volatile organic compounds and those of high molecular mass. It is used in for the analysis of proteins, peptides, glycoproteins, oligosaccharides, and oligonucleotides.

MALDI is based on the usage of matrix complexed with a given sample molecule that is bombarded with a laser in order for the sample molecule to form a sample ionization. The sample is normally mixed into a high absorbable matrix with as little matrix as possible as the matrix will also become excited and come off and ionize as well. The matrix itself acts as a substance which infuses the sample as well as a transformer for the laser's energy into excitation energy to allow for the vaporization of the sample ions and matrix ions from the surface of the matrix. Most commercially available MALDI mass spectrometers are now a pulsed nitrogen laser of wavelength 337 nm. This method is normally coupled with a Time of Flight detector in order to obtain proper charge-mass ratios and calculate a mass spectrum.

Samples for this procedure are prepared based on retaining homogeneous MALDI sample. This would include focusing on the concentration of the matrix and analyte, the choice of matrix, the analyte sample history, such as how its exposure to strong ionic detergents and formic acid may affect it, also hydrophobicity or hydrophilicity of both the matrix and sample, and possible contaminants and compatible solubilities of matrix and analyte solutions.

SELDI-TOF
Surface Enhanced Laser Desorption Ionization is a modification of the procedure used in MALDI. Instead of mixing the UV sensitive matrix with the protein sample, the protein sample is spotted on a plate which has some surface binding characteristics such as a chromatographic array. The spots are then washed to remove impurities and weakly bound proteins. The UV matrix is then added to the spot and allowed to co-crystallize. After the ionization with the UV laser, the ions are analyzed using a TOF mass analyzer, in the same manner as MALDI.

SELDI provides on-chip separation as well as the capability to perform enzymatic reactions directly on the chip. However, there are concerns about the reproducibility of SELDI-TOF mass spectra, especially when normal post processing techniques frequently used with MALDI such as baseline correction are applied. Environmental sources of variation such as humidity can also play a large role.(http://bioinformatics.oxfordjournals.org/cgi/screenpdf/20/5/777 Baggerly et al. 20 (5): 777. (2004))

Tandem MS
Tandem Mass spectrometry (MS/MS) is spectrometer used to separate ions based on a sample's "electronic" mass using two or more quadrupoles. A sample is normally coupled into tandem MS via chromatography method, normally an electron spray method like gas chromatography or liquid chromatography where the contents are volatilized. More popular tandem mass spectrometers are quadrupole-quadrupole, magnetic sector-quadrupole, and the quadrupole-time-of-flight geometries (P. Roepstorrf, 1989)

The Tandem MS is constructed of two or more quadrupoles, with a collision cell separating each quadrupole. Once a sample has been separated by chromatography, the substances initially go through an initial quadrupole which separates the mixture of ions allotting only certain ions (Pre-cursor ions), passage to the collision cell. The first quadropole is used to select user-specified sample ions from a specific component; usually the molecular-related (i.e (M+H)+ or (M-H)-) ions. Within the collision cell the Precursor-ions also known as "Parent ions" are then bombarded with an inert gas (Xe, Ar, ect ) and are further broken down into different charged and mass ions (Product ions). These product ions also known as "Daughter ions" are then run through an additional quadrupole to further separate the ions which is set to monitor specific ion fragments. This process can be repeated several times in order to get highly specific readings.

In peptide sequencing, selected ion components are either positive (M+H)+ or negative (M-H)- ions. The selected ions will pass into the collision cell, there are three different types of bonds that can fragment along the amino acid backbone: NH-CH, CH-CO, and CO-NH. For each of these fragments, the charge can be maintained by either the N or C-terminal fragment. There are actually six different types of fragments that can be formed. The mass difference between two fragments of the same type is indicative of a particular amino acid.

This technique is primarily used with peptide sequencing due to the parent-daughter ion scanning. Due to the two ions being scanned initially as a precursor and product ion, a mass fingerprinting can occur where through further analysis and investigation the fragments of ions can be pieced together to determine a peptide sequence. Since it is known that amino acid backbone fragments among the NH-CH, CH-CO, and CO-NH bonds, each type of bond can give rise to six different type of species, and these can then be pieced together to provide peptide fragmentation.

TIMS (Thermal Ionization-Mass Spectrometry)
TIMS (Thermal Ionization-Mass Spectrometry) is a mass spectrometer that can make exact measurements of isotope ratios of thermally ionizable elements. This ionization can be done by passing them through metal ribbons under vacuum. The resulting ions are accelerated by electrical potential gradient and they are focused into a beam using electrostatically charged plates and slits. The beam is passed through a magnetic field and based on the m/z ratio the original beam produces many separated beams. Using collectors, these separated beams are converted into voltage and exact isotope ratios can be obtained by comparing these beams to their individual ion beams.

SSMS (Spark Source Mass Spectrometry)
SSMS (Spark Source Mass Spectrometry) can ionize the analytes in solid samples using electric current with two electrodes. It works as one electrode if the sample is metal or can be placed in a cup-shaped electrode by mixing with graphite.

Rarely used Mass Spectrometry Ionization Types

 * Fast Atom Bombardment (FAB): A technique where the anylate is bombarded with highly charged atoms in a vacuum under in a non-volatile matrix.
 * Soft laser desorption (SLD): Often referred to as Desorption/Ionization on Silicon (DIOS), is the process by which large macro-molecules are ionized without fragmentation.
 * Atmospheric pressure chemical ionization (APCI): A form of chemical ionization unique in that the entire procedure may be performed in atmospheric pressure.
 * Secondary ion mass spectrometry (SIMS): A technique which allows for the inspection of solid surfaces via an ion beam disassociation technique called sputtering.
 * Spark ionization (SI): Sometimes referred to by the antiquated term spark source ionization, this method allows for the generation of gaseous phase ions from a solid surface.
 * Thermal ionization (TI): Often referred to as Surface Ionization, where an anylate is ionzaed from a matrix or filament, usually a metal disk.


text:
Proteomics/Protein Identification - Mass Spectrometry/Instrumentation

This Section:

How does a Mass Spectrometer work?
A mass spectrometer is made up of three components: an ion source, mass analyzer, and a detector. The unknown sample which may originate as solid, liquid, solution or vapor, is presented to the ionization source. After ionizing the sample, the ions of the sample are passed to the mass analyzer region where separation based on the mass-to-charge ratio occurs. Once separated by the analyzer, the ions then enter the detector portion of the mass spectrometer. At this point, the machine calculates the mass-to-charge ratio and the relative abundance of each of the different ions. From this information, a spectrum graph can be created such as the one to the right.

Most mass spectrometers are maintained under a vacuum to improve the chances of ions traveling from ionization source to detector without interference by collision with air molecules.

Ion Source
The ion source is the mass spectrometer component which ionizes the sample to be analyzed. Ionization mainly serves to present the sample as vaporized ions which can be acted upon by the mass analyzer and measured by the ion detector. There are many different methods available to ionize samples, such as positive or negative ion modes. The ionization method chosen should depend on the type of sample and the type of mass spectrometer.

Ionization Methods: There are three types of ionization methods, electron ionization, chemical ionization and photo-induced ionization. Electron ionization involves application of an electrical current to the sample to induce ionization. Chemical ionization involves interaction of the sample with reagent molecules to induce ionization. Ions produced are often denoted with symbols that indicate the nature of the ionization, eg. [M+H]+ is used to represent a molecule which is protonated.

 * Electron ionization
 * Electrospray Ionization
 * Field Desorption / Field Ionization
 * Chemical Ionization
 * Matrix Assisted Laser Desorption Ionization
 * Fast Atom Bombardment
 * Thermal Ionisation

The methods commonly used in proteomics are ‘Matrix Assisted Laser Desorption Ionization’ or MALDI and ‘Electrospray Ionization’ also known as ESI. Atmospheric pressure chemical ionization and Atmospheric pressure photo-ionization are two other forms as well.

MALDI uses a solid support target plate where a UV active matrix (solid or liquid) is spotted on the plate followed by the sample over the matrix. The laser hits the spot on the crystallized matrix and transfers energy from the matrix molecule to the sample. This energy transfer vaporizes the sample, sending a plume of ions into the MALDI source. This plume of ions is then collected and held in the source until a pulse sends them all out simultaneously. If the MALDI is attached to a Time of Flight(TOF) mass analyzer these ions are then sent down the TOF tube (typically ~2m) and are separated according to their velocity (light ions hitting first). MALDI is the preferred instrumentation for proteomics due to ease of reading the spectrum; most ions are found in the +1 charge state [M+H].

Electrospray, on the other hand, is done by injecting the sample dissolved in a slightly acidic solution through a heated capillary that has a voltage around 10v. This allows for highly charged particles to be formed at the tip of the capillary. As the particles evaporate, their charge/volume increases to a point where charge repulsion forces take over and the particle will explode. A small drop will form which continues the process until individual molecules are in the gas phase and charged. These ions will then travel into the analyzer, typically a quadrupole, to be scanned one mass at a time. The molecules in electrospray tend to be multiply charged and even though the upper mass limit of a quadrupole is 2000 m/z, the multiple charges allow for high mass ions or proteins to be identified. Proteins will have a charge envelope in which each peak has a different amount of charges on them. Special software is needed to deconvolve the multiple charge species peaks into a single mass peak, such as MassLynx from Waters. This form of ionization is good for most compounds, although is not best with neutral or low polarity molecules.

Atmospheric pressure chemical ionization involves interaction of the sample with reagent molecules to induce ionization. As in electrospray ionization, liquid is pumped through a capillary. At the tip it is nebulized and a corona discharge takes place ionizing the molecules. The molecules interact with the analyte and transfer their charge. This form of ionization is good for small thermally stable molecules.

Atmospheric pressure photo-ionization uses photons to excite and ionize the molecules after they have been nebulized. This form of ionization is good for neutral compounds.

Mass Analyzers
The mass analyzer is the component that separates the ions created from the ion source by their mass-to-charge ratios. Mass analyzers are based on the principles of charged particles in an electric or magnetic field. By using Lorentz force law and Newton’s second law of motion you can generate the following equation:

$$(\frac{m}{q}) \mathbf{a} = \mathbf{E}+ \mathbf{v} \times \mathbf{B}$$

Where m is the mass, the ionic charge is q, a the acceleration, E is the electric field, and the vector cross product of the ion velocity and the magnetic field is v x B.  This equation says that two particles with the same mass to charge ratio (m/q) will behave exactly the same.

So what this equation is basically saying is that the mass to charge ratio acts as a determinant of acceleration of the ion, which can also be represented as the addition of the electric field plus the cross product of the ion velocity and magnetic field.

Scanning Mass Analyzers
Scanning mass analyzers need to separate the ions based on their relative abundances and mass to charge ratios. Electromagnetic fields are used to separate the ions based on their mass to charge ratios, by using a slit they are able to regulate which mass to charge ratio ions get to the detector. Once selected for a particular mass to charge ratio, the ion current is then recorded as a function of time which is analagous to mass.

Sector Mass Spectrometer
Mass spectrometer that uses a mass analyzer using magnetic, electric or static sector in it is called a sector instrument. This also works in combination of sectors like BEB, magnetic-electric-magnetic. In the present days, these sector instruments are mostly double focusing i.e, the ion beams are focused in both direction and velocity. Here is how a magnetic sector mass spectrometer works, imagine a tube like thing between two electromagnets. When the electrons are passed through the tube from one end to another the magnetic field bends the electron stream by exerting turning force on it. Then m/z ratio is determined.

Orbitrap Mass spectrometer
Orbitrap Mass spectrometer is the one in which ions are subjected to an electric field produced by electrodes tangentially. Also these ions are trapped between outer electrodes, where as ions are attracted with an electrostatic attraction to the inner electrode which is balanced by centrifugal force. Therefore these ions move in a circular manner around the inner electrode also back and forth with a particular m/z ratio. By using this ion oscillation based on the m/z ratio, the trap can act as a mass analyzer.

Quadrupole Mass Spectrometers
You can think of this method as a filter or funnel which only allows certain ion masses to pass through. The "funnel" is actually a combination of positively and negatively charged metal rods which together form a channel through which the ions travel. The theory is that only selected masses will be able to pass through the channel, as all other ions won't have a stable trajectory though it and will hit the quadrupole rods, stopping the ion from reaching the detector.

Ion trap Quadrupole Spectrometer
A quadrupole ion trap mass spectrometer consists of hyperbolic electrodes with a ring and two endcaps, which is the core of this instrument. In this method, ions are trapped and then sequentially ejected into a conventional electron multiplier detector from the ion trap. That way all ions can be stored during the process of mass analysis. Recent findings showed that using 1 mtorr of helium gas in the trapping volume substantially improved the resolution of the instrument with the kinetic energy of the ions reducing and the ion trajectories contracted to the center of the trap. A packet can be formed with a given m/z ions. This spectrometer is used widely for commercial purposes because of the high resolution and it is inexpensive.

Linear Quadrupole Mass Spectrometer
In the linear ion trap mass spectrometer the ions are trapped within a set of quadrupole rods to hold the ions radially and end electrodes to maintain the ions axially with a static electrical potential. It is simply said that unlike Quadrupole Ion Trap, which uses a 3-D field, Linear Quadrupole Ion Trap uses a 2-D field. It has a selective mass filter that detects the ions of particular m/z ratio. This method has advantages like higher ion storage capacity and faster scanning technique.

Time of Flight Mass Analysers
The TOF (Time of Flight) is a mass analyzer that allows ions to flow down a field free region; which allows the ions with a greater velocity, lighter ions, to hit the detector first. This is especially compatible with MALDI due to the fact that the TOF needs a pulsed instrument for its source. In this way ions are generated in the MALDI source and held there for a brief time and all are pulsed into the TOF at the same exact time. In this way, If all ions have the same kinetic energy, the ions with the lower mass will have a higher velocity and reach the detector first; whereas the ions with the higher mass will have a lower velocity and hit the detector last.

The kinetic energy of an ion leaving a source if given by:

$$ T=eV= \frac{mv^2}{2} $$

Where velocity v is defined by the Length of the path L divided by time t.

$$ v= \frac{L}{t} $$

By substituting this equation into the first and solving for time you arrive at.

$$t=L * \sqrt{( \frac{m}{e})*( \frac{1}{2V})}$$

From this equation you can easily see how mass directly affects travel time. Mass is directly proportional to time. Using the m/e portion of the equation you can clearly see how a larger mass means a longer time, and likewise how a lower mass would mean a smaller m/e and thus shorter travel time.

Ion Cyclotron Resonance Spectrometer
ICR is a form of trapped Ion mass analyzer, that specifically is defined as a static trap. It is basically a box with three parallel metal sides. Trapped ion analyzers work by keeping the ions in the trap and controlling the ions by using positive and negatively charged electrical fields in a carefully series of timed events.

ICR specifically works on the principle that in a magnetic field, ions move in a circular path whose frequency is mass dependent. So using the cyclotron frequency you can surmise the mass. Equating the Lorentz force in a magnetic field to the equation for centripetal force yields.

$$ evB= \frac{mv^2}{r} $$

You can then easily solve the above equation for the frequency F or    $$ F= \frac{v}{r} $$

Groups of ions with the same mass to charge ratios will have the same cyclotron frequency but may be moving out of synch with one another, this is why an excitation pulse is needed to bring the resonant ions into phase with one another and the excitation pulse. Next the ions which will be passing close to the ICR cell receiver plates cause "image currents" which can be collected and amplified and analyzed. This signal registered in the receiver plates depends both on the number of ions and their distances from the receiver plates.

Fourier transformation
This mass spectrometry includes a mass analyzer that uses cyclotron frequency of the ions to determine their m/z ratio. Here a magnetic field with electric trapping plates known as penning trap is used to hold the ions. An oscillating electric field with the magnetic field at right angle to it is used to excite the trapped ions to a larger cyclotron radius. This results in packets of oscillating ions. The trapping plates detects the signal as a image current and results in a interferogram with sine waves called free induction decay (FID). By performing a Fourier transform to this data, a mass spectrum can be generated with useful signal.

Detector
Those ions which pass through analyzer are now separated by the desired methods. This mass spectrometry component records the charge induced by an ion passing by a surface or current produced when an ion hits a surface. From these charges or currents, a mass spectrum can be produced as well as measure the total number of ions at each each m/z which are present. Due to the fact that the number of ions entering the detector at any given moment is minuscule, signal amplification is often necessary.

Next section: Types of Mass Spectrometry

Principles and Applications of Liquid Chromatography-Mass Spectrometry in Clinical Biochemistry
[http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2643089 Pitt JJ. The Clinical Biochemist Reviews Volume:3019-34 (2009) ]

Main Focus
One benefit of Liquid Chromatography - Mass Spectrometry is there are different configurations to allow for results more geared toward the experiment.

Summary

LC-MS was slow to take off due to inefficient technologies. However, in the mid 1990’s, after new technologies were developed, it became more popular. This was in part due to its high specificity and ability to handle more complex mixtures than the other options available at the time, such as GC-MS. Mass spectrometry starts by ionizing samples to generate charged molecule fragments then analyzing their mass to charge-ratio. There are different technologies used to perform the mass spectrometry part of LC-MS to obtain different results, some being more versatile than others, such as changing the ion source, changing the mass analyzer, changing the ion suppression as well as changing the direct injection method.

Different ion sources that can be used clinically would be an electrospray ionization source, an atmospheric pressure chemical ionization source or an atmospheric pressure photo-ionization source. Electrospray ionization, also known as ESI, works well on polar molecules; metabolites, xenobiotics and peptides are some examples. Atmospheric pressure chemical ionization source, also known as APCI, is great analyzer for small thermally stable molecules and neutral non-polar molecules such as free steroids. Atmospheric pressure photo-ionization, also known as APPI, works well with neutral compounds such as steroids.

There are four different types of mass analyzers that can be used; these are the quadrupole analyzers, time-of-flight analyzers, ion trap analyzers, and hybrid analyzers. Quadrupole analyzers are are widely used because their ease of scanning and good quality quantitative data. Time-of-flight analyzers are used for small molecules because of its high sensitivity. Ion trap analyzers have the ability to fragment an ionize ions several times giving so-called MSn capabilities. Hybrid analyzers can be switched between ion trap mode and conventional quadrupole mode.

There are also different steps that can be changed in the Liquid Chromatography part of LC-MS to make the procedure more versatile such as changing the flow rate, the mobile phase, the resolution and through-put and the quantitation (calibration). The parameters and conditions involved in LC-MS can be changed to optimize the assay. However, these conditions are specific to the particular analyte and the LC separation. Therefore there are no general conditions. Some of these conditions include using a dilute solution of the analyte and using single MS or tandem MS. It is also important to make sure the LC-MS system is working properly with protocols to detect deviations from normal performance. LC-MS is used in the Biochemical screening for genetic disorders as well as therapeutic drug monitoring and steroid hormones.

New Terms

 * GC-MS: Gas chromatography-mass spectrometry (GC-MS) is a method that combines the features of gas-liquid chromatography and mass spectrometry to identify different substances within a test sample. ( http://en.wikipedia.org/wiki/GC-MS)
 * Ion source: A device in which gas ions are produced, focused, accelerated, and emitted as a narrow beam. Also known as ion gun; ionization source. ( http://www.answers.com/topic/ion-source )
 * Calibration: a set of graduations to indicate values or positions —usually used in plural  ( http://www.merriam-webster.com/dictionary/calibration )
 * Deviation: noticeable or marked departure from accepted norms of behavior ( http://www.merriam-webster.com/dictionary/deviation )
 * Xenobiotics: a chemical compound (as a drug, pesticide, or carcinogen) that is foreign to a living organism ( http://www.merriam-webster.com/dictionary/xenobiotics )

Course Relevance

 * How is this applicable to the proteomics class?

It is important to be able to analyze what makes up a protein so that we can understand the affects of that protein on an organism. Being able to see the differences between a given protein and its normal counterpart could help in the understanding of genetic diseases. LC-MS gives scientists the ability do protein separation.

What is Mass Spectrometry?
Chiu CM, Muddiman DC. http://www.asms.org/whatisms/index.html (3/28/09)

Main Focus
This website discusses what mass spectrometry is, the history behind it, and how it works.

Summary
Mass spectrometry is a powerful analytical technique that is used to identify unknown compounds, to quantify known compounds, and to elucidate the structure and chemical properties of molecules. Compounds can be identified at very low concentrations. Mass spectrometry is used by a wide range of professionals such as physicians, astronomers, and biologists. For example it can monitor the breath of patients by anesthesiologists during surgery and determine the composition of molecular species found in space. It can be used to identify structures of biomolecules as well sequence them. It is also used to identify and quantitate compounds of complex organic mixtures. Mass spectrometry was invented by J.J. Thomson in a vacuum tube. His invention was used to discover a number of isotopes, to determine the relative abundance of the isotopes, and to measure their "exact masses" which are important in the foundation for later developments in diverse fields ranging from geochronology to biochemical research.

A mass spectrometer is an instrument that measures the masses of individual molecules that have been converted into ions by becoming electrically charged. A mass spectrometer does not actually measure the molecular mass directly, but rather the mass-to-charge ratio of the ions formed from the molecules. The charge on an ion is denoted by the integer number of the fundamental unit of charge, and the mass-to-charge ratio. It represents daltons per fundamental unit of charge. Results are in a generated mass spectrum. A mass spectrum is a graph of ion intensity as a function of mass-to-charge ratio.

New Terms

 * dalton: a unit of mass for expressing masses of atoms, molecules, or nuclear particles equal to 1⁄12 of the atomic mass of the most abundant carbon isotope ( http://www.merriam-webster.com/medical/dalton )
 * corona: a faint glow adjacent to the surface of an electrical conductor at high voltage ( http://www.merriam-webster.com/dictionary/corona )
 * mass spectrum: the spectrum of a stream of gaseous ions separated according to their differing mass and charge ( http://www.merriam-webster.com/dictionary/mass%20spectrum )
 * elucidate: to make lucid especially by explanation or analysis ( http://www.merriam-webster.com/dictionary/elucidate )
 * isotopes: any of two or more species of atoms of a chemical element with the same atomic number and nearly identical chemical behavior but with differing atomic mass or mass number and different physical properties ( http://www.merriam-webster.com/dictionary/isotopes )

Course Relevance

 * How is this applicable to the proteomics class?

Proteomics is the study of the protein and is defined as the qualitative and quantitative comparison of proteomes under different conditions to further unravel biological processes. Mass spectrometry allows for the study of the components of an organism and how they create their individual functions.