The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways.

ABSTRACT: Conformational dynamics play critical roles in protein folding, misfolding, function, misfunction, and aggregation. While detecting and studying the different conformational states populated by protein molecules on their free energy surfaces (FESs) remain a challenge, NMR spectroscopy has emerged as an invaluable experimental tool to explore the FES of a protein, as conformational dynamics can be probed at atomic resolution over a wide range of timescales. Here, we use chemical exchange saturation transfer (CEST) to detect "invisible" minor states on the energy landscape of the A39G mutant FF domain that exhibited "two-state" folding kinetics in traditional experiments. Although CEST has mostly been limited to studies of processes with rates between ∼5 to 300 s^-1 involving spars

SUBMITTER: Tiwari VP 

PROVIDER: S-EPMC8609552 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature