Protein conformational populations and functionally relevant substates

Accounts of Chemical Research
Arvind RamanathanPratul K Agarwal

Abstract

Functioning proteins do not remain fixed in a unique structure, but instead they sample a range of conformations facilitated by motions within the protein. Even in the native state, a protein exists as a collection of interconverting conformations driven by thermodynamic fluctuations. Motions on the fast time scale allow a protein to sample conformations in the nearby area of its conformational landscape, while motions on slower time scales give it access to conformations in distal areas of the landscape. Emerging evidence indicates that protein landscapes contain conformational substates with dynamic and structural features that support the designated function of the protein. Nuclear magnetic resonance (NMR) experiments provide information about conformational ensembles of proteins. X-ray crystallography allows researchers to identify the most populated states along the landscape, and computational simulations give atom-level information about the conformational substates of different proteins. This ability to characterize and obtain quantitative information about the conformational substates and the populations of proteins within them is allowing researchers to better understand the relationship between protein structure and ...Continue Reading

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Related Concepts

Protein Conformation
Computational Molecular Biology
Cyclophilin A
Biocatalysis
Allosteric Regulation
Pharmaceutical Preparations
Ligands
Magnetic Resonance Imaging
Research Personnel
Chemical cofactor

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