The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme.

ABSTRACT: The biological function of a protein is intimately related to its structure and dynamics, which in turn are determined by the way in which it has been folded. In vitro refolding is commonly used for the recovery of recombinant proteins that are expressed in the form of inclusion bodies and is of central interest in terms of the folding pathways that occur in vivo. Here, biophysical data are reported for in vitro-refolded hydrogenated hen egg-white lysozyme, in combination with atomic resolution X-ray diffraction analyses, which allowed detailed comparisons with native hydrogenated and refolded perdeuterated lysozyme. Distinct folding modes are observed for the hydrogenated and perdeuterated refolded variants, which are determined by conformational changes to the backbone structure of the L

SUBMITTER: Ramos J 

PROVIDER: S-EPMC8647175 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature