Amino Acids and Properties

Can be phosphorylated

Ser, Thr, Tyr - have OH group

Positively charged

Basic AA’s - H (forms a ring), K (lysine), R

Negatively charged

Acidic AA’s - D (aspirate), E (glutamate)

Can be acetylated

K (lysine)

rigid and kinky structure, helix breaker

P

At the beginning of all proteins

Met

Has an inverse V type branching at the end

V, L, N (Asparagine), Q (glutamine)

can make disulfide bridges

C

Smallest hydrophobic amino acid

Ala

Have big bulky hydrophobic rings

Aromatics- F, Y, W (Trp)

Smallest amino acid

G

Has the biggest ring

W

When lysine has a CH3- CO added to the side chain

Ac-K

Lysine mutated to prevent acetylation

R

S or T mutated to prevent phosphorylation

Ala

Tyrosine mutated to study phosphorylation

F

Has a sulfur atom

Met, Cys

Hydrophilic, but does not have a charge, nor can be phosphorylated

N (asparagine), Q (glutamine)

has NH2’s for H Bonding

N (asparagine), Q (glutamine)

Mutations mimicking phosphorylation

S,Y, or T → D (aspirate) or E (glutamate)

Mutations mimicking acetylation

K (lysine)→Q (glutamine)

Forms Helices

M(methionine) A (alanine) L (leucine) K(lysene) R(argenine)

Forms beta sheets

F (phenylalanine), Y (tyrosine), W (Triptophan)

Forms beta turns

rigid proline makes a kink, flexible glycine obeys it