Impact of local unfolding fluctuations on the evolution of regional sequence preferences in proteins.

ABSTRACT: The number of distinct structural environments in the proteome (as observed in the Protein Data Bank) may belie an organizing framework, whereby evolution conserves the relative stability of different sequence segments, regardless of the specific structural details present in the final fold. If true, the question arises as to whether the energetic consequences of amino acid substitutions, and thus the frequencies of amino acids within each of these so-called thermodynamic environments, could depend less on what local structure that sequence segment may adopt in the final fold, and more on the local stability of that final structure relative to the unfolded state. To address this question, a previously described ensemble-based approach (the COREX algorithm) was used to define proteins in te

SUBMITTER: Voortman-Sheetz K 

PROVIDER: S-EPMC11837041 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature