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Covalent chemical bonds.. Through condensation reaction .. Link is peptide linkage Molecule formed amide Can be broken down with hydrolysis..
Essential
Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Threonine Tryptophan
Nonessential
Alanine Arginine Aspartic acid Cysteine Glutamic acid Glutamine Glycine Proline
Valine
Serine Tyrosine
Asparagine Selenocysteine
Can be synthesized in the body Not required in diet Can be formed from a-keto acids by transamination and subsequent reactions
R Group
Shape
Polarity/Charge
Aliphatic
Aromatic
Polar, uncharged
Nonpolar
Polar Uncharged
Polarity / charge
1. Nonpolar amino acids Only carbon and hydrogen in their side chains. Generally unreactive but hydrophobic. 2. Polar amino acids Polar amino acids are those with side-chains that prefer to reside in an aqueous (i.e. water) environment. For this reason, one generally finds these amino acids exposed on the surface of a protein.
Alanine (Ala) Phenylalanine (Phe) Valine (Val) Proline (Pro) Leucine (Leu) Tryptophan (Trp) Isoleucine (Ile)
http://www.indstate.edu/thcme/mwking/amino-acids
Threonine (Thr)
Asparagine (Asn)
Tyrosine (Tyr)
Glutamine (Gln)
http://www.indstate.edu/thcme/mwking/amino-acids.h
Two amino acids with negatively charged (i.e. acidic) side chains - Aspartate (Aspartic acid) and Glutamate (Glutamic acid).
These amino acids confer a negative charge on the proteins of which they are part.
Lysine and Arginine both have pKs around 10.0 and are therefore always
positively charged at neutral pH.
Less hydrophobic
More hydrophobic
Formation of proteins
Formation of biologically active compound like thyroxin, melanin, adrenalin, IAA, Coenzymes etc.
Formation of glucose
Formation of amines
Nitrogen storage
Antibiotics
Biological buffers
A peptidoglycan cell wall composed of disaccharides and amino acids gives bacteria structural support.