CHEM 451 Lecture Notes - Lecture 17: Coiled Coil, Groel, Beta Sheet
Document Summary
Focusing on groes mutation, 71 tyr to his or arg in 2 variants (mutations can alter chemical envionrment of folding chamber/ allosterically affect groel) Substitutions/ mutations change electrostatics, polar molecules have an effect on it. If they had anything that was charged or polar -> increase in function of protein. If they have something that is non polar -> decrease protein function. Because this is a single ring structure, you increase 7 residues, so it"s a big point mutation since it"s a large assembly. When mixed/match groel and es, wanted to see if things worked better, 3-2 with wt has good enhancement of folding, but not much better than 3-2 with 3-1, none are as good as their original formation. Major conclusions about this work: engineered specificity that interacted with native substrates. Improving ability of groel/es to fold gfp comes at the price of it acting as a general molecular chaperone - gfp optimised chaperonins can have growth defects.
