Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.

ABSTRACT: Proteins naturally occur in crowded cellular environments and interact with other proteins, nucleic acids, and organelles. Since most previous experimental protein structure determination techniques require that proteins occur in idealized, non-physiological environments, the effects of realistic cellular environments on protein structure are largely unexplored. Recently, Förster resonance energy transfer (FRET) has been shown to be an effective experimental method for investigating protein structure in vivo. Inter-residue distances measured in vivo can be incorporated as restraints in molecular dynamics (MD) simulations to model protein structural dynamics in vivo. Since most FRET studies only obtain inter-residue separations for a small number of amino acid pairs, it is important to dete

SUBMITTER: Liu Z 

PROVIDER: S-EPMC11568256 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature