A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.

ABSTRACT: The journey by which proteins navigate their energy landscapes to their native structures is complex, involving (and sometimes requiring) many cellular factors and processes operating in partnership with a given polypeptide chain's intrinsic energy landscape. The cytosolic environment and its complement of chaperones play critical roles in granting many proteins safe passage to their native states; however, it is challenging to interrogate the folding process for large numbers of proteins in a complex background with most biophysical techniques. Hence, most chaperone-assisted protein refolding studies are conducted in defined buffers on single purified clients. Here, we develop a limited proteolysis-mass spectrometry approach paired with an isotope-labeling strategy to globally monitor the

SUBMITTER: To P 

PROVIDER: S-EPMC9860312 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature