Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.

ABSTRACT: Proteins are dynamic entities that intermittently depart from their ground-state structures and undergo conformational transitions as a critical part of their functions. Central to understanding such transitions are the structural rearrangements along the connecting pathway, where the transition state plays a special role. Using NMR relaxation at variable temperature and pressure to measure aromatic ring flips inside a protein core, we obtain information on the structure and thermodynamics of the transition state. We show that the isothermal compressibility coefficient of the transition state is similar to that of short-chain hydrocarbon liquids, implying extensive local unfolding of the protein. Our results further indicate that the required local volume expansions of the protein can occu

SUBMITTER: Dreydoppel M 

PROVIDER: S-EPMC8395657 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature