Mapping Multiple Distances in a Multidomain Protein for the Identification of Folding Intermediates.

ABSTRACT: The investigation and understanding of the folding mechanism of multidomain proteins is still a challenge in structural biology. The use of single-molecule Förster resonance energy transfer offers a unique tool to map conformational changes within the protein structure. Here, we present a study following denaturant-induced unfolding transitions of yeast phosphoglycerate kinase by mapping several inter- and intradomain distances of this two-domain protein, exhibiting a quite heterogeneous behavior. On the one hand, the development of the interdomain distance during the unfolding transition suggests a classical two-state unfolding behavior. On the other hand, the behavior of some intradomain distances indicates the formation of a compact and transient molten globule intermediate state. Furth

SUBMITTER: Cerminara M 

PROVIDER: S-EPMC7002912 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature