Exploring the sequence and structural determinants of the energy landscape from thermodynamically stable and kinetically trapped subtilisins: ISP1 and SbtE.

ABSTRACT: A protein's energy landscape, all accessible conformations, their populations, and dynamics of interconversion, is encoded in its primary sequence. While how a protein's primary sequence encodes its native state is well understood, how sequence encodes the kinetic barriers such as unfolding and refolding is not. Here we have looked at two subtiliase homologs from the Bacillus subtilis, Intracellular Subtilisin Protease 1 (ISP1) and Subtilisin E (SbtE), that are expected to have very different dynamics. As an intracellular protein, ISP1 has a small pro-domain thought to act simply as a zymogen, whereas the extracellular SbtE has a large pro-domain required for folding. The stability and kinetics of ISP1 and ProSbtE have been previously characterized. We now directly compare their ene

SUBMITTER: Hood MR 

PROVIDER: S-EPMC11419036 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature