20 Amino Acids Flashcards
(22 cards)
G
Glycine Gly
Nonpolar, aliphatic R group, chiral
A
Alanine Ala
Nonpolar, aliphatic R group, hydrophobic
P
Proline Pro
Nonpolar, aliphatic R group, “cis” amino acid makes kinks in alpha helices and often used in beta turns
V
Valine Val
Nonpolar, aliphatic R group, hydrophobic
L
Leucine Leu
Nonpolar, aliphatic R group, hydrophobic
I
Isoleucine Ile
Nonpolar, aliphatic R group, hydrophobic, isomer of leucine
M
Methionine Met
Nonpolar, aliphatic R group, hydrophobic, start codon
S
Serine Ser
Polar uncharged R group, hydrophilic, can be phosphorylated
T
Threonine Thr
Polar uncharged R group, hydrophilic, can be phosphorylated
C
Cysteine Cys
Polar uncharged R group, covalent disulfide binds, mildly hydrophilic
8.3
N
Asparagine Asn
Polar uncharged R group, hydrophilic
Q
Glutamine Gln
Hydrophilic
F
Phenylalanine Phe
Aromatic R groups, hydrophobic, aromatic
Y
Tyrosine Tyr
Aromatic R groups, mildly hydrophobic, can be phosphorylated
10
W
Tryptophan Trp
Aromatic R groups, hydrophobic
D
Aspartate Asp
Negatively Charged R groups, negative charge
Below 4
E
Glutamate Glu
Negatively charged R group, negative charge
Above 4
K
Lysine Lys
Positively charged R groups
10.5 (10.8)
R
Arginine Arg
Positively charged R groups, guanadino
12.5
H
Histidine His
Positively charged R groups, base, uncharged physiological
6
Primary structure
Primary structure linear chain amino acids, linked by peptide binds between carboxyl and amines, amino acids referred to as residues. Exposed amino group at N terminus left and c terminus on right. Residues dictate how fold
Secindary structure
Alpha helices and beta sheets formed by h bonds
Alpha helices carbonyl oxygen and amide hydrogen for intramolecular bonds at core so side chains outwards.
Beta sheets parallel or antiparallel, rows held by intramolecular h binds with carbinyl and amid h bonds.
