ProGuide: a flexible framework for modeling global conformational rearrangements in proteins using DEER-derived distance restraints.

ABSTRACT: Conformational heterogeneity is integral to protein function - ranging from enzyme catalysis to signal transduction - and visualizing distinct conformational states requires experimental techniques capable of providing such structural information. One particularly powerful method, double electron-electron resonance (DEER) spectroscopy, can provide a high-resolution, long-range (~15-80 Å) probability distributions of distances between site-selected pairs of spin labels to resolve intra-protein distance parameters of unique protein conformations, as well as their respective likelihoods within a conformational ensemble. A current frontier in the field of DEER spectroscopy is utilizing this distance information in computational modeling to generate complete structural models of these multiple

SUBMITTER: Grosskopf JD 

PROVIDER: S-EPMC12258946 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature