proteins

what are the hydrophobic (non-polar) amino acids

glycine, alanine, valine, leucine, isoleucine, methionine, proline

name the two hydrophobic (non-polar) amino acids with aromatic rings

phenylalanine and tryptophan

what are the hryophilic (polar, charged) amino acids

aspartate, glutamate, lysine, arginine, histidine

name the hydrophilic (polar, neutral) animo acids

asparagine, glutamine, theronine, cysteine

what is the modifications seen in serine and threonine

O-linked glycosylation (glycoprotein), reversible phosphorylation (ser/the kinases)

what is a modification seen in asparagine

N-linked glycosylation

what is a modification seen in proline (ring)

forces bend in protein structure. can be hydroxylated like collagen

what are the 4 different levels of protein structures

primary, secondary, tertiary, quaternary

what is a primary(1y) structure of a protein

amino acid sequence

what is a secondary(2y) structure of a protein

local structure of polypeptide chain H bonding between carbonyl oxygen and amide hydrogen

what the two types of secondary (2y) structures

alpha helix and beta sheets

what is a tertiary (3y) structure of a protein

side chain interactions, biologically active proteins

what types of bonds happen at the tertiary(3y) level

h bonding, electrostatic interactions between charged groups, hydrophobic interactions, van der waal’s forces, disulfide bonding between cysteine residues strong interaction

what is a quaternary(4y) structure of a protein

complex of 2 or more separate polypeptide chains interactions between subunits. non-covalent and covalent interaction.

what is an example of a quaternary(4y) structure of a protein

hemoglobin, a 4 subunit interacting structure

what can cause a protein to denature

disrupting bonds, heat, pH, detergents and organic solvents (hydrophobic bonds), chaotropic agent

how does chaotropic agents denature proteins

urea or guanidine form H bonds with AAs and disrupts existing H bonds and hydrophobic interactions

how does pH denature proteins

affects H boning and electrostatic interactions

how does heat denature proteins

breaking weak bonds like egg whites

why is it important for the primary structure to be correct

it can cause gene mutations if it is damaged

Describe the structure of collagen

triple helix stabilized by H bonds, 3 AA per turn, glycine occupies every 3rd position, proline and hydroxyproline to exterior, small

what is scurvy

a vitamin C deficiency (ascorbate)

what is vitamin C

a co-enzyme for prolyhydroxylase

how can scurvy effect collagen

insufficient hydroxylation of proline, fewer H bonds therefore becomes unstable

what is Osteogenesis imperfecta

mutation in Gly codon Collagen unstable due to genetic condition

what are prion diseases

scrapies, BSE, CWD, CJD

How is scrapies formed

change from globular form of protein to fibrous form of protein

how do you apply proteomics

difference in protein profile, qualitative- difference in amino acid sequence and quantitative- increase or decrease in proteins