Effects of ionic strength on the folding and stability of SAMP1, a ubiquitin-like halophilic protein.

ABSTRACT: Our knowledge of the folding behavior of proteins from extremophiles is limited at this time. These proteins may more closely resemble the primordial proteins selected in early evolution under extreme conditions. The small archaeal modifier protein 1 (SAMP1) studied in this report is an 87-residue protein with a β-grasp fold found in the halophile Haloferax volcanii from the Dead Sea. To gain insight into the effects of salt on the stability and folding mechanism of SAMP1, we conducted equilibrium and kinetic folding experiments as a function of sodium chloride concentration. The results revealed that increasing ionic strength accelerates refolding and slows down unfolding of SAMP1, giving rise to a pronounced salt-induced stabilization. With increasing NaCl concentration, the rate of fold

SUBMITTER: Mizukami T 

PROVIDER: S-EPMC8874027 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature