Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR.

ABSTRACT: Protein dynamics are an intrinsically important factor when considering a protein's biological function. Understanding these motions is often limited through the use of static structure determination methods, namely, X-ray crystallography and cryo-EM. Molecular simulations have allowed for the prediction of global and local motions of proteins from these static structures. Nevertheless, determining local dynamics at residue-specific resolution through direct measurement remains crucial. Solid-state nuclear magnetic resonance (NMR) is a powerful tool for studying dynamics in rigid or membrane-bound biomolecules without prior structural knowledge with the help of relaxation parameters such as T ₁ and T _1ρ. However, these provide only a combined result of a

SUBMITTER: Chevelkov V 

PROVIDER: S-EPMC10037497 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature