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Fold, Degrad, Polymo
WVSOM Class of 2012 Protein Folding, Degradation, and Polymorphism
| Question | Answer |
|---|---|
| helper proteins that overcome kinetic barriers are called? | heat shock proteins (isomerases) |
| heat shock proteins are also called what? | chaperonins |
| what proteins are involved in folding? | prolyl cis/trans isomerases, protein disulfide isomerases, and disulfide reductases |
| what molecule cleaves peptide bonds in front of aromatic amino acids? | chymotrypsin |
| to degrade proteins, what molecule is added? | ubiquitin |
| what is the ligand that binds to proteins and causes ubiquitin to attach? | E3 |
| glycation aggregates are called what? | advanced glycation end products (AGES) |
| HbA1C is a measure of what? | hemoglobin glycosylation |
| what are two major aberrations of protein folding? | prion's disease and alzheimer's disease |
| is an isoform the same or different gene? what about a mutation? | different, same |
| ck is important in regenerating what? | atp |
| what happens to intracellular ck when it is elevated? | it diffuses out of the cell |
| HbF has increased oxygen affinity why? | decreased 2,3-BPG binding |
| HbF gamma chains have what AA instead of serine? | histidine |
| collagens have many ____ which lead to diseases? | polymorphisms |
| what are the 2 human prion diseases? | creutzfeldt-jakob disease and variant cjd |
| protein misfolding can cause the _____ that lead to alzheimer's disease? | plaques |