Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.

ABSTRACT: The chaperonin GroEL binds non-native polypeptides in an open ring via hydrophobic contacts and then, after ATP and GroES binding to the same ring as polypeptide, mediates productive folding in the now hydrophilic, encapsulated cis chamber. The nature of the folding reaction in the cis cavity remains poorly understood. In particular, it is unclear whether polypeptides take the same route to the native state in this cavity as they do when folding spontaneously free in solution. Here, we have addressed this question by using NMR measurements of the time course of acquisition of amide proton exchange protection of human dihydrofolate reductase (DHFR) during folding in the presence of methotrexate and ATP either free in solution or inside the stable cavity formed between a single ring variant

SUBMITTER: Horst R 

PROVIDER: S-EPMC2410080 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature