Amino Acids, Peptides, and Protein I Flashcards
Hydrophobic and non-polar amino acids
Valine Isoleucine Leucine Methionine Phenylalanine Tryptophan Cystine (LIMP- TV Channel)
hydrophilic and polar amino acids
argenine lysine aspartate glutamate asparagine glutamine
acidic amino acids
aspartate
glutamate
basic amino acids
lysine
arginine
histidine
what may interactions between positive and negative R groups form?
salt bridge important for stabilization in proteins
what is a disulfide bond?
covalent linkage between two sulfer atoms specifically between cystine residues (thiol groups)
which amino acid has a sulfur bond but cannot participate in a disulfide bond?
methionine
where are disulfide bonds usually found within a folded protein?
on the inside because they are hydrophobic
what are the 6 major post-translational modifications that we need to know?
- hydroxylation of proline
- carboxylation of glutamate
- modification by acetylation or methylation
- glycosylation
- reversible phosphorylation/dephosphorylation
- ubiquination
what adds a hydroxyl group to proline residue?
prolyl hydroxylase
what is the predominate secondary structure in collagen and how is it formed?
proline helix
formed by multiple prolines and hydroxyprolines in a row
what is the cofactor of prolyl hydroxylase?
vitamin C
what disease results as a lack of vitamin C and which structure is affected?
scurvy, loss of integrity in connective tissues becase lack of proline hydroxylation
which enzyme adds a carboxyl group to the side chain of glutamate?
Gamma-glutamyl carboxylase
what is the co-factor of carboxylation of glutamate?
vitamin K
where is carboxylation of glutamate mostly found?
within clotting factors
what will a lack of vitamin K cause in regards to carboxylation of glutamate?
hemorrhage
how does waafarin work?
blood thinner that prevents clotting by inhibiting activity of gamma-glutamyl carboxylase