Challenges in describing the conformation and dynamics of proteins with ambiguous behavior.

ABSTRACT: Traditionally, our understanding of how proteins operate and how evolution shapes them is based on two main data sources: the overall protein fold and the protein amino acid sequence. However, a significant part of the proteome shows highly dynamic and/or structurally ambiguous behavior, which cannot be correctly represented by the traditional fixed set of static coordinates. Representing such protein behaviors remains challenging and necessarily involves a complex interpretation of conformational states, including probabilistic descriptions. Relating protein dynamics and multiple conformations to their function as well as their physiological context (e.g., post-translational modifications and subcellular localization), therefore, remains elusive for much of the proteome, with studies to i

SUBMITTER: Roca-Martinez J 

PROVIDER: S-EPMC9382080 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature