BIOL3150 Lecture Notes - Hydrolysis, Proteasome, Proinsulin
Document Summary
Ribonucleases can denature and refold in solutions without any help from other proteins, enzymes can reform on its own. Polypeptide can become temporarily trapped in a semi-stabled. Cells utilize chaperones, proteins that help other proteins to fold conformation state properly: groel/groes chaperonin aids folding of proteins (uses hydrolysis of 7 atp molecules, sense misfold protein from hydrophobic paths (unfold, proteolytic cleavage protein) Inactive preproinsulin and requires several cleavages and formation of disulfide bond to convert to convert it to a fully active form: cleavge, formation of disulfide bond (proinsulin), cleave again (insulin, chemical modifications. Secretory proteins are often glycosylated with sugar moieties: most excess or unwanted proteins in eukaryotes are removed by ubiquitin- dependent proteasome degradation pathway.
