Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.

ABSTRACT: Water is key to protein structure and stability, yet the relationship between protein-water interactions and structure is poorly understood, in part because there are few techniques that permit the study of dehydrated protein structure at high resolution. Here, we describe liquid-observed vapor exchange (LOVE) NMR, a solution NMR-based method that provides residue-level information about the structure of dehydrated proteins. Using the model protein GB1, we show that LOVE NMR measurements reflect the fraction of the dried protein population trapped in a conformation where a given residue is protected from exchange with D₂O vapor. Comparisons to solution hydrogen-deuterium exchange data affirm that the dried protein structure is strongly influenced by local solution stability and

SUBMITTER: Crilly CJ 

PROVIDER: S-EPMC8603359 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature