Primary structure
sequence of aa in polypeptide chain
linear, aa joined by peptide bonds
Secondary structure
driven primarily by peptide backbone interactions
stabilized by H bonds
alpha helix/beta sheet
Tertiary structure
driven primarily by side-chain interactions
fold w hydrophobic side chains sheltered inside
Quaternary structure
2 or more chains combine
Amino acid structure
COO-
|
H3N+\_\_ Calpha \_\_H
|
R (side chain)Chirality
any molecules whose reflection in a mirror cannot be superimposed
attached: 4 non-identical groups
L-chirality
L-aa rotates polarized light to the left
***only glycine achiral
Peptide bond
formed by a nucleophilic addition-elimination reaction between the carboxyl and amino groups of adjacent amino acids
rigid, planar bond due to resonance delocalization of e-
not a lot of rotation
N-terminal
beginning
amino group
C-terminal
end
carboxyl group
Non-polar, aliphatic aa
Gly (G), Ala (A), Pro (P), Val (V), Leu (L), Ile (I), Met (M)
Polar, uncharged R groups
Ser (S), Thr (T), Cys (C), Asn (N), Gln (Q)
- can form HBs w water/ other polar mol
- Ser, Thr: found on pr- surface
OH of serine great nucleophile
- Cys: polar side chain form HBs w water, found on pr- surface, SH group great nucleophile
- Asn, Gln: amide counterparts to Asp/Glu, have nonionizable uncharged polar side chains
Aromatic R groups
Phe (F), Tyr (Y), Trp (W)
Negatively charged R groups
Asp (D), Glu (E)
Positively charged R groups
Lys (K), Arg (R), His (H)
Multisubunit proteins
Oligomeric vs protomers
2/more polypeptides associated noncovalently
Oligomeric: if at least 2 are identical
Protomers: identical units
Simple protein
contains only aa resides and no other chemical constituents
Conjugate protein
prosthetic group
contain permanently associated chemical components in addition to aa
Prosthetic group: non-amino acid part