Amino Acids

ALA

Alanine (A)

ARG

Arginine (R)

ASP

Aspartic Acid (D)

• aka aspartate (salt)

ASN

Asparagine (N)

CYS

Cysteine (C)

GLU

Glutamic aicd (E)

• aka glutamate (salt)

GLN

Glutamine (Q)

GLY

Glycine (G)

HIS

Histidine (H)

ILE

Isoleucine (I)

LEU

Leucine (L)

LYS

Lysine (K)

MET

Methionine (M)

PHE

Phenylalanine (F)

PRO

Proline (P)

SER

Serine (s)

THR

Threonine (T)

TRP

Tryptophan (W)

TYR

Tyrosine (Y)

VAL

Valine (V)

Aliphatic Amino Acids (6)

• Glycine

• alanine

• valine

• leucine

• isoleucine

• proline

Aliphatic properties

• open hydrocarbon side chains

• low dielectric constant

• nonpolar

• hydrophobic

• found in interior of proteins

• 
  

Aromatic (3) FYW

• Phenylalanine

• Tyrosine

• Tryptophan

Aromatic properties

• ring-containing side chains

• hydrophobic (Tyrosine is less bc of -OH)

• Phe and Trp are nonpolar

• Tyr is polar

Sulfer-Containing (2) CM

• Cysteine

  • contains a reactive sulfhydryl (SH) group

• Methionine

Aliphatic + Hydroxyl (2) ST

• serine

• Threonine

Aliphatic + Hydroxyl properties

• hydrocarbon side chain with -OH group

• O-H bond has a dipole → side chains are more polar than reg aliphatic or aromatic chains

• polar, neutral hydropathy

Basic (3) KRH

• Lysine

• Arginine

• Histidine

Basic properties

• N-H has large dipole moment → side chains are hydrophilic

  • found on soluble proteins’ exteriors

  • polar, charged, hydrophilic

• at neutral pH → chains are proton acceptors (+ charge)

Acidic (2) DE + Uncharged Derivatives (2) NQ

• aspartate

• glutamate

• asparagine

• glutamine

Acidic properties (DE)

• acidic side chains, proton donors

• at neutral pH, they are negatively charged

• polar, hydrophilic

Uncharged Derivatives (NQ)

• amide rather than a carboxylate in the side chain, making them uncharged.

• polar, hydrophilic