-
Alanine
- Ala
- A
- hydrophobic, nonpolar, no acid/ base or H bond
-
Arginine
- Arg
- R
- Most basic aa, does H bonds, poor nuc, pka 12.5
-
Asparagine
- Asn
- N
- Polar, H bonds, not nuc, no acid/base prop
-
Glycine
- Gly
- G
- smallest aa, nonpolar, no acid/base or H bond
-
-
Leucine
- Leu
- L
- "like valine only Larger"
-
-
Proline
- Pro
- P
- Not hydrophobic, constrained in rotation
- "PRO LINE- huddled around ball"
-
Serine
- Ser
- S
- Not acid/base, hydrophilic, polar, H bonds
-
Threonine
- Thr
- T
- no acid/base, hydrophilic, polar, h bonds
-
Cysteine
- Cys
- C
- 2 cys can bind to each other (stabilize protein structure), poor H bond, acid/base (can dissociate)
-
Methionine
- Met
- M
- Thioether, hydrophobic, initiator aa in proteins
-
Phenylalanine
- Phe
- F
- very hyrdophobic, large (affects protein structure)
- Aromatic!
-
Tyrosine
- Tyr
- Y
- reactive side chain, h bonds, hydrophobic, acid/base, "tire-o-sine"
- Aromatic!
-
Tryptophan
- Trp
- W
- Largest aa, least common, h bond, no acid/base
- Aromatic!
-
Histidine
- His
- H
- base, + charge at neutral pH, salt bridges/h bonds, hydrophilic, rare, at active sites. pka=6
-
Lycine
- Lys
- K
- salt bridge, h bond, hydrophilic, nucleophile, pka=10.5 (pH=7)
-
Glutamate
- Glu
- E
- hydrophilic, h bonds and salt bridges, often at active sites
- pka=4.2
-
Gluamine
- Gln
- Q
- polar, h bonds, no acid/base, not nucleophile
-
Aspartate
- Asp
- D
- hydrophilic, h bonds and salt bridges, often at active sites
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