A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.

ABSTRACT: The folding pathways of large proteins are complex, with many of them requiring the aid of chaperones and others folding spontaneously. Along the folding pathways, partially folded intermediates are frequently populated; their role in the driving of the folding process is unclear. The structures of these intermediates are generally not amenable to high-resolution structural techniques because of their transient nature. Here we employed single-molecule force measurements to scrutinize the hierarchy of intermediate structures along the folding pathway of the nucleotide binding domain (NBD) of Escherichia coli Hsp70 DnaK. DnaK-NBD is a member of the sugar kinase superfamily that includes Hsp70s and the cytoskeletal protein actin. Using optical tweezers, a stable nucleotide-binding comp

SUBMITTER: Bauer D 

PROVIDER: S-EPMC5939067 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature