BIO 205 PROTEIN STRUCTURE Flashcards
polypeptides are
chains of amino acids linked by peptide bonds
amino acid formula
H | H2N -- C -- COOH | R
R= side-chain group
unique R groups defining..
specific amino acids
amino acid at pH 7
H | (+) H3N -- C -- COO (-) | R
formation of a polypeptide via peptide bond
pics
condensation of 2 amino acids == dipeptide
together by amide linkage
- remove 1 water molecule
Polar amino acids - Hydrophilic/Hydrophobic
Hydrophilic
NonPolar amino acids - Hydrophilic/Hydrophobic
Hydrophobic
Asparatic acid
[Asp]
acidic
neg polar, hydrophilic
Glutamic acid
[Glu]
acidic
neg polar, hydrophilic
Arganine
[Arg]
basic
pos polar, hydrophilic
Lysine
[Lys]
basic
pos polar, hydrophilic
Histidine
[His]
basic
pos polar, hydrophilic
Asparagine
[Asn]
uncharged polar, hydrophilic
Glutamine
[Glu]
uncharged polar, hydrophilic
Serine
[Ser]
uncharged polar, hydrophilic
Threonine
[Thr]
uncharged polar, hydrophilic
Tyrosine
[Tyr]
uncharged polar, hydrophilic
Alanine
[Ala]
non polar, hydrophobic
Glycine
[Gly]
non polar, hydrophobic
SMALLEST ; only H
Valine
[Val]
non polar, hydrophobic
Leucine
[Leu]
non polar, hydrophobic
Isoleucine
[Ile]
non polar, hydrophobic
Proline
[Pro]
non polar, hydrophobic
Phenylalanine
[Phe]
non polar, hydrophobic
Methionine
[Met]
non polar, hydrophobic
Tryptophan
[Trp]
non polar, hydrophobic
Cysteine
[Cys]
non polar, hydrophobic
unfolded protein
- disordered, high entropy
- few non covalent (enthalpies) interactions
folded protein
- highly ordered, low entropy
- many non covalent interactions
forces that determine protein folding into its native 3-D structure
- covalent bonding
- hydrogen bonding
- van der waals
- hydrophobic effects