Amino Acids Properties and Alphabet

Alanine

Ala, A

Cystine

Cys, C

Aspartic Acid

Asp, D

Glutamic Acid

Glu, E

Phenylalanine

Phe, F

Glycine

Gly, G

Histidine

His, H

Isoleucine

Ile, I

Lysine

Lys, K

Leucine

Leu, L

Methionine

Met, M

Asparagine

Asn, N

Proline

Pro, P

Glutamine

Gln, Q

Arginine

Arg, R

Serine

Ser, S

Threonine

Thr, T

Valine

Val, V

Tryptophan

Trp, W

Tyrosine

Tyr, Y

Polar Uncharged

STQNYC

Polar charged

Aspartic acid, glutamic acid, lysine, arginine, histidine

Glycine property

flexible and can tightly pack, side chain consists only of hydrogen atom and can fit into either a hydrophobic or hydrophilic environment. Often resides at sites where two polypeptides come into close contact.

Cysteine property

disulfide bond formation. side chain has polar, uncharged character but has unique property of forming a covalent bond with another cysteine to form a disulfide link

Proline property

breaks secondary structure, side chain has hydrophobic character but has the unique property of creating kinks in polypeptide chains and disrupting ordered secondary structure

Positive charged

Arginine, Histidine, Lysine

Negative charged

Aspartic acid, glutamic acid

hydrophobic side chains

alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, tryptophan

Helix forming

leucine, methionine and Glutamate

Helix breakers

Proline and Glycine

Beta sheet formers

isoleucine, valine and phenylalanine

Make up active site

SHEDKC