Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus.

ABSTRACT: Salt-bridges play a key role in the thermostability of proteins adapted in stress environments whose intrinsic basis remains to be understood. We find that the higher hydrophilicity of PfP than that of HuP is due to the charged but not the polar residues. The primary role of these residues is to enhance the salt-bridges and their ME. Unlike HuP, PfP has made many changes in its intrinsic property to strengthen the salt-bridge. First, the desolvation energy is reduced by directing the salt-bridge towards the surface. Second, it has made bridge-energy more favorable by recruiting energetically advantageous partners with high helix-propensity among the six possible salt-bridge pairs. Third, ME-residues that perform intricate interactions have increased their energy contribution by making majo

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC8172842 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature