Conserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states.

ABSTRACT: The native folding of certain zymogen-derived enzymes is completely dependent upon a prosegment domain to stabilize the folding transition state, thereby catalyzing the folding reaction. Generally little is known about how the prosegment accomplishes this task. It was previously shown that the prosegment catalyzes a late-stage folding transition between a stable misfolded state and the native state of pepsin. In this study, the contributions of specific prosegment residues to catalyzing pepsin folding were investigated by introducing individual Ala substitutions and measuring the effects on the bimolecular folding reaction between the prosegment peptide and pepsin. The effects of mutations on the free energies of the individual misfolded and native ground states and the transition state we

SUBMITTER: Dee DR 

PROVIDER: S-EPMC4077824 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature