CHEM 451 Study Guide - Final Guide: Groel, Rhodanese, Groes
Document Summary
Groel/es = e. coli chaperonin, homooligomeric complex arranged in 2x7 stacked rings, cochaperonin groes (heptameric ring that binds to both end of groel) Nb groel 3 domains: apical = binds groes/ substrates, equatorial = atp binding site, inter subunit domains. Intermediate hinge domain for increase cavity/ create polar environment. Can fold substrates that aren"t similar in sequence, structure, function. Want to see if chaperonin can be selective based off wide range of selection. Conclusion = optimising of groel/es to fold gfp comes at a price of losing general molecular chaperone function/ growth defects. Gfp = non native substrate, jellyfish, still works in groel/es. Optimised gfpwt -> gfpopt as wt inefficient folding when overexpressed. Proved that gfp folded more because of groel (not increase in gfp conc itself) Dna shuffling variation = random/ fragment -> recombine targeted mutagenesis within one organism"s dna ->
