Multilevel superposition for deciphering the conformational variability of protein ensembles.

ABSTRACT: The dynamics and variability of protein conformations are directly linked to their functions. Many comparative studies of X-ray protein structures have been conducted to elucidate the relevant conformational changes, dynamics and heterogeneity. The rapid increase in the number of experimentally determined structures has made comparison an effective tool for investigating protein structures. For example, it is now possible to compare structural ensembles formed by enzyme species, variants or the type of ligands bound to them. In this study, the author developed a multilevel model for estimating two covariance matrices that represent inter- and intra-ensemble variability in the Cartesian coordinate space. Principal component analysis using the two estimated covariance matrices identified the

SUBMITTER: Amisaki T 

PROVIDER: S-EPMC10983786 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature