The change of conditions does not affect Ros87 downhill folding mechanism.

ABSTRACT: Downhill folding has been defined as a unique thermodynamic process involving a conformations ensemble that progressively loses structure with the decrease of protein stability. Downhill folders are estimated to be rather rare in nature as they miss an energetically substantial folding barrier that can protect against aggregation and proteolysis. We have previously demonstrated that the prokaryotic zinc finger protein Ros87 shows a bipartite folding/unfolding process in which a metal binding intermediate converts to the native structure through a delicate barrier-less downhill transition. Significant variation in folding scenarios can be detected within protein families with high sequence identity and very similar folds and for the same sequence by varying conditions. For this reason, we h

SUBMITTER: Grazioso R 

PROVIDER: S-EPMC7713307 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature