Asparagine

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Chemical formula:

-C4H8N2O3

·      Abbreviations:

-N

-Asn

·      Codons:

-AAU

-AAC

·      First amino acid to be isolated.

·      First isolated in 1806 by French chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet.

·      Contains a carboxamide group.

·      It is a non-essential amino acid so the body can synthesize it, however, it is found in the following foods:

-dairy, whey, beef, poultry, eggs, fish, lactalbumin, seafood, asparagus, potatoes, legumes, nuts, seeds, soy and whole grains.

·      Was first isolated in crystalline form from asparagus juice.

·      Plays an important role in the synthesis in ammonia.

·      Polar, uncharged

·      A reaction occurs between asparagine and reducing sugars that forms acrylamide in food when heated to sufficient temperature.  This is found in baked goods such as French fries, potato chips and toasted bread.

Valine

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Subgroup:

branched-chain amino acid

Special features:

 In individuals with sickle-cell disease, Valine substitutes for glutamic acid in hemoglobin.  Valine is hydrophobic causing hemoglobin to be prone to abnormal aggregation.

Charge:

nonpolar, not charged

Abbreviations:

Val or V

Bonus Fun Facts:

•       Codons are GUU, GUC, GUA, and GUG.

•       Named after the plant valerian

Histidine

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·      Abbreviations: H (His)

·      Basic Group

·      Polar (Positively Charged)

·      Only 2 Codons: CAU and CAC

·      Used for rheumatoid arthritis, allergic diseases, and anemia

·      Involved in many metabolic processes in the body.

·      Essential and nonessential amino acid

·      Needed especially in children and infants for proper growth and development

·      When metabolized in the body, it produces Histamine which is involved in inflammatory response and HCl in the stomach

·      If infants do not eat enough of this amino acid, they may develop eczema

http://www.livestrong.com/article/517676-what-foods-contain-histidine/

http://www.webmd.com/vitamins-supplements/ingredientmono-467-HISTIDINE.aspx?activeIngredientId=467&activeIngredientName=HISTIDINE

Lysine

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Abbreviated : Lys, K

Charge: positive (polar)

Basic

Codes: AAA and AAG

Essential Amino Acid in humans, found in protein.

-       Plays an essential role in the production of carnitine, a nutrient responsible for converting fatty acids into energy and helping to lower cholesterol

-       Help with calcium absorption

-       Need for proper growth

-       Not enough lysine can cause fatigue, nausea, dizziness, loss of appetite, agitation, bloodshot eyes, slow growth, anemia, and reproductive disorders.

Usage

-       Can help with Herpes Simplex Virus and Osteoporosis

Isoleucine

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·       Chemical formula: HO₂CCH(NH₂)CH(CH₃)CH₂CH₃

·       Abbreviations: I, Ile

·       Essential branched-chain aliphatic amino acid – cannot be synthesized by humans, must be ingested (nuts, seeds, meat, eggs, fish, lentils, peas, soy protein)

·       Important for hemoglobin synthesis and regulation of blood sugar & energy levels

·       Deficiency: headaches, dizziness, fatigue, depression, confusion, & irritability

·       Charge: neutral

·       Codons: AUU, AUC, AUA

·       Hydrophobic

·       Felix Ehrlich discovered isoleucine in hemoglobin in 1903

·       Chiral (non-superimposable mirror image) side chain

·       Synthesized from 2-bromobutane and diethylmalonate

·       4 stereoisomers, 2 diastereomers (not mirror images) from L-isoleucine

·       In nature: (2S,3S)-2-amino-3-methylpentanoic acid

Cysteine

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C

Cys

·      Polar (uncharged) Amino Acid

·      Common in protein binding and active sites and can act as a nucleophile ( reactive center of an enzyme)

·      Forms disulfide bridges with other cysteine molecules that stabilize protein structure

·      Intracellular Cysteines often bind to metals

Sources:

http://www.chem4kids.com/files/aminoacids/cysteine.html

Arginine

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·      Abbreviations: Arg and R

·      Semi essential amino acid

·      Side chain: guanidine

·      Polar charge

·      Designed to bind phosphate anion

·      Found in active centers of proteins that bind phosphorylated substrates

·      Important in cell division, healing wounds, removing ammonia from the body, immune function, release of hormones

o   Long term memory, circulation, reproductive system

·      Precursor for synthesis of nitric oxide: which help arteries relax and improve blood flow

·      First extracted from the Lupine seedling

·      Found in soybeans, chicken, coconuts, dairy products, chickpeas etc.

·      Amounts of arginine produced in the body decreases as we age

Glycine

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Gly, G

• Smallest amino acid

• Side chain is one hydrogen

• Nonpolar zwitterion

• Not chiral

• Almost 1/3 of collagen is composed of Glycine

• Biosynthesized

·      Abbreviations:  Glu and E

·      Negatively charged and polar

·      Pka of R group is 4.3

·      Non-essential

·      White crystalline

·      Soluble in water

·      Found in brain and spinal cord

·      Increase the firing of neurons in the nervous system

·      Important in the metabolism of fats

·      One of the only nutrients capable of detoxifying ammonia in the brain

Essential amino acid

     Distinguishing characteristic- contains an indole functional group

     It belongs to the aromatic amino acid subgroup

     Tryptophan does not have a charge

     Abbreviation- Trp or W

     Tryptophan is found in food, and helps with the production of serotonin and melatonin (it helps you sleep)

For this reason, tryptophan has been associated with the post- Thanksgiving meal stupor you feel after stuffing yourself with turkey.  Tryptophan is probably not the true culprit in this case, because it works better on an empty stomach.  Tryptophan is the least abundant of the amino acids. As long as you get your daily requirement of meat (which contains a good serving of tryptophan) you will likely meet your daily requirement. There are 2 isomers of tryptophan, L and D, but your body only uses the L-stereoisomer.

Methionine

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(M)

Met

Side chain very hydrophobic

Facts:

·      The initiating AA

·      1 of 2 AA’s that contain SULFUR

·      First Isolated in 1992

·      One of the essential AA’s

·      Crucial in methylation process (sourse of name)

·      1 of 3 AA’s that is responsible for production of creatine (energy) in the body

·      Also helps remove trace amounts of heavy metals

·      Methionine promotes healthy skin, and healthy hair and nail growth

·      Lack of Methionine will lead to many problems à most interesting: dementia like symptoms

Leucine

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·      Leucine abbreviated as Leu or the single letter is L.

·      Leucine is classified as a hydrophobic amino acid due to its aliphaticisobutyl side chain.

·      Leucine is a  white, crystalline, water-soluble amino acid, the linear structure is  C 6  H 13  NO 2

·      Leucine is an essential amino acid, meaning that the human body cannot synthesize it, and it therefore must be ingested.

·      Leucine is utilized in the liver, adipose tissue, and muscle tissue.

·      Leucine is negatively charged. 

Tyrosine

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Single letter abreviation: Y

-Three letter abreviation: Tyr

-Nonessential amino acid with a Polar Side group

-"Tyrosine" comes from the Greek word tyri which meas cheese, as it was first discovered in 1846 by a German Chemisty in the    protein casein from cheese

-Occurs in proteins that are part of signal transduction proceses

-Functions as a receiver of phosphate groups that are transferred by protein kinases

-Codons are UAC and UAU

-Dietary Sources: chicken, turkey, fish, peanuts, almonds, avocados, milk, cheese, yogurt, cottage cheese, lima beans, pumpkin seeds, sesame seeds, bananas, and soy products

-A number of studies have found Tyrosine to be useful during conditions of stress, cold, fatigue, loss of a loved one, prolonged sleep deprivation; tyrosine does not seem to have any significant effect on mood, cognitive or physical performance in normal circumstances.

Cysteine

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Abbreviation:  Cys , C

Chemical Formula: HO2CCH(NH2)CH2SH

Codons: UGU, UGC

Not charged, Polar

One of two, Sulfur containing Amino Acids.  (The other is Methionine)

Semi –essential amino acid is biosynthesized in the liver as long as Met is available

Side chain (Thiol, R- S-H) can serve as a nucleophile and can easily be oxidized

Can act as an acid or base.

 Forms Disulfide bonds w/ other Cysteine molecules.  Can help stabilize extracellular proteins and cell membranes.

Powerful antioxidant.  Can be used to reduce the harmful effects of alcohol, smoking and pollution

Binds to easily to metals to help the body eliminate them.

Found in high protein foods as well as; garlic, onions, red peppers, broccoli, brussels sprouts, and sprouted lentils.

Adenine (A) is one of the four bases of DNA among cytosine, guamine, and thymine.  Its chemical formula is C₅H₅N₅.  In DNA, Adenine always binds with thymine with two hydrogen bonds.  Adenine is a purine whereas thymine is a pyrimidine. In RNA, Adenine binds with uracil instead.  Adenine is present in all living organisms because it is a base that helps to form nucleotides, which give structure to DNA chains. 

Glutamine

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Glutamine (Q, Gln)

-Polar, neutral charge

-most abundant amino acid in the body

-stored in muscle, made in lungs

-important for removing excess ammonia

-nonessential

-used to counteract side effects of medical diseases/treatments (ex: cancer, digestive problems, HIV, AIDS, surgical problems)

-necessary to repair wounds by providing nitrogen

-only amino acid capable of crossing the blood/brain barrier

Phenylalanine

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Phenylalanine (abbreviated as Phe or F) is an essential amino acid.  It is found in the breast milk of mammals.  It is hydrophobic due to the benzene ring and electrically neutral.  It’s codons are UUU and UUC.  It is a precursor for tyrosine (your body has an enzyme that turns phenylalanine into tyrosine), which controls signaling molecules for dopamine, norepinephrine, epinephrine (adrenaline) and melanin.  Some symptoms of deficiency are confusion, lack of energy, depression, decrease of alertness, memory problems, and lack of appetite.   At birth (usually within 48-72 hours), infants are tested to make sure they have the enzyme required to turn phenylalanine into tyrosine.  If they don’t, the condition is called phenylketonuria (PKO).   If not caught within the first 3 weeks of life, phenylalanine will build up in the baby, causing severe, irreversible retardation.  If caught right away the child can be fine with dietary restrictions.  They need to avoid phenylalanine and take tyrosine supplements to have optimum brain development and growth.

Proline

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Proline (Pro or P are its abbreviations)

1.    Non-polar

2.    The ring structure is very important in the function of the amino acid with a protein.

3.    Often found at the end of an α-helix or in a loop or turn.

4.    Not an essential amino acid; can be produced in the human body from glutamic acid.

5.    Its codons are CCU, CCC, CCA, and CCG

http://www.newworldencyclopedia.org/entry/Proline

Cytosine

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Cytosine is a nucleic acid. This nitrogenous base is located in both DNA and RNA and as a pyrimidine it pairs with guanine in Watson-Crick base pairing. Three hydrogen bonds form between these two bases.

• Abbreviation: C
• Chemical formula: C₄H₅N₃O
• Negatively charged
• Highly unstable and can spontaneously change into uracil which then can lead to point mutations.

Alanine, abbreviated Ala or A, is a nonpolar (uncharged, hydrophobic) amino acid. Alanine is a non essential amino acid that is the second highest amino acid occurring second only to leucine. Alanine is involved in the Glucose-Alanine cycle which occurs during the times when muscles produce lactate during times of decreased oxygen, they also produce alanine which is then transferred to the liver where it is used to make glucose.

Serine

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One letter abbreviation of Serine is S, and the three letter abbreviation is Ser. Serine is one of the proteinogenic amino acids. Serine is one of two amino acids in the hydroxyl group. Serine is polar (uncharged) and hydrophilic. Serine has a density of 1.60 g/cm^3. Serine’s codons in the genetic code are UCU, UCC, UCA, UCG, AGU and AGC. Serine is a non-essential amino acid because it can be synthesized in the body from other metabolites. It’s important in metabolism because it participates in the biosynthesis of purines and pyrimidine. Serine is a precursor to the amino acids glycine, cysteine and tryptophan in bacteria, as well as the metabolites sphingolipids and folate. Serine also plays an important role in the catalytic function of many enzymes. Serine proteases is a common type of protease.  

Taurine

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Taurine is not technically an amino acid because it only contains and amino group but no carboxyl group.  It is found mostly in bile and the large intestines.  It is a major component of building skeletal muscle, cardiovascular health, and central nervous system development.  Taurine is a sulfonic acid, which is different from the other amino acids found in the body.  It was first isolated by ox bile in 1827.  Even though taurine is a naturally biological molecule in the body elevated levels of taurine are banned by the NCAA for athletes.  The reason is because it is a stimulant that can work like a steroid in building muscle.

http://en.wikipedia.org/wiki/Taurine

Thymine

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the T in A,T,G,C - - the 4 bases usually found in DNA

It is a pyrimadine (as are Cytosine and Uracil)

Adenine is its Watson-Crick base pair partner, with which it forms 2 hydrogen bonds

It is replaced by Uracil in RNA

UV light can damage DNA by forming Thymine dimers