Amino acid Letter 3 letter Group Notes At PH 7

Glycine G Gly non polar, Not optically active. Very small, in bends and twists
aliphatic, On the inside of proteins bc hydrophobic
N.E hydrophobic

Alanine A Ala non polar, Soluble in water but more hydrophobic than glycine.
aliphatic, On the inside of proteins bc hydrophobic
N.E hydrophobic

Valine V Val non polar, 5 C (V) and in the V shape. Interior core bc
aliphatic, hydrophobic. On the inside of proteins bc hydrophobic
E hydrophobic

Leucine L Leu non polar, Valine with an extra CH2 in the stem, 6 C total. On the
aliphatic, inside of proteins bc hydrophobic
E hydrophobic

Isoleucine I Ile non polar, Valine with an extra methyl on end, iso= next to alpha.
aliphatic, On inside of proteins bc hydrophobic, does this more
E hydrophobic than other hydrophobic bc its a larger aliphatic group

Methionine M Met non polar, S in the middle - subjective to oxidation and reduction.
aliphatic, Protein denatures a lot bc of free radicals oxidize S,
E hydrophobic which is a thioester. Start codon, so in every protein.
inside of proteins bc hydrophobic, does this more than
other hydrophobic bc its a larger aliphatic group

Proline P Pro non polar, The alpha amino group also attached to side chain, does
aliphatic, not exist in many proteins bc of this conformational
N.E hydrophobic restriction. On the inside of proteins bc hydrophobic,
more so bc aromatic

Phenylalanine F Phe Aromatic , Has a phenyl ring in place of the methyl hydrogen
hydrophobic atoms on alanine and is nonpolar. Since its
E hydrophobic it clusters together in the inside of the
protein (hydrophobic effect, stronger in aromatic)

Tryptophan W Trp Aromatic, Has an indole ring with two fused rings and an NH2
hydrophobic group joined to a methylene (CH2). is nonpolar. Since
E its hydrophobic it clusters together in the inside of the
protein (hydrophobic effect- stronger in aromatic)

Tyrosine T Tyr Aromatic, Has OH group on a ring, making it more acidic than
(non polar polar bc it other aa with alc (S/T). places where body attaches
counter = N.E contains an e phosphate for intracellular signaling. electrons in the O
phenylalanine) neg atom — H bond are attracted to the oxygen atom, making it
ionizable side partially negative, which in turn makes the hydrogen
chain partially positive (similar to F but w/ OH on ring)
Threonine T Thr Polar, Has an alcohol group. places where body attaches
(non polar uncharched, phosphate for intracellular signaling. electrons in the O
counter = valine​) E has OH — H bond are attracted to the oxygen atom, making it
partially negative, which in turn makes the hydrogen
partly positive

Serine S Ser Polar, Has an OH group (in place of valine methyl) and is
(non polar uncharched, aliphatic. Places where body attaches phosphate for
counter = N.E contain eneg intracellular signaling. e- in the OH bond are attracted
alanine) atom and OH to the oxygen atom, making it partially negative, which
in turn makes the hydrogen partly positive

Cystine C Cys Polar, Like serine but has an SH (so it can do redox). Can
uncharched, completely lose a proton at slightly basic pH to form
ionizable side N.E contain eneg the reactive thiolate group. Pairs of sulfhydryl groups in
chain atom close proximity may form disulfide bonds

Asparagine N Asn Polar, Acidic -- aspartic acid has four C. has a carboxyl and
uncharched, amino aka carboxamide (terminal)
ionizable side N.E contain eneg
chain atom

Glutamine Q Gln Polar, Acidic -- glutamic acid which has 5 C . has a carboxyl
uncharched, and amino aka carboxamide (terminal)
ionizable side N. E contain eneg
chain atom

Aspartate D Asp Negatively negatively charged under intracellular conditions.i n

(like asparagine charged, some proteins, these side chains accept protons, which
but COOH not N. E acidic side neutralize the negative charge
carboxamide​) chain

Glutamate E Glu Negatively negatively charged under intracellular conditions. in

(like glutamine charged, some proteins, these side chains accept protons, which
but COOH not N. E acidic side neutralize the negative charge
carboxamide) chain

Arginine R Arg Positively terminate with groups that are positively charged at
charged, neutral pH.
ionizable side N. E Hydrophilic
chain

Lysine K Lys Positively terminate with groups that are positively charged at
ionizable side charged, neutral pH. topped by an amino group and arginine by a
chain E Hydrophilic guanidinium group

Histidine H His Positively Has an imidazole group, (aromatic ring that can be +
charged, charged). Pka near 6, so imidazole group of H is unique
ionizable side E Hydrophilic in that it can be uncharged or positively charged near
chain neutral pH. Found in the active sites of enzymes, where
the imidazole ring can bind and release protons in the
course of enzymatic reactions