From Solution to Gas Phase: Revealing Ligand-Dependent Conformations of Ribonuclease A with Tandem-Trapped Ion Mobility Spectrometry.

ABSTRACT: Protein activity depends on motional transitions between conformational states. Modifications or ligand binding can alter the protein dynamics, leading to changes in activity. Established biophysical methods effectively determine protein structures but face challenges when investigating dynamic biological processes that involve steady states of transiently populated conformations. Ion mobility/mass spectrometry shows promise for studying transient protein conformations but characterizes them in a solvent-free environment and does not directly provide detailed structural information. Here, we investigate to what extent subtly different conformational states are retained in their solvent-free environment. We investigate the conformations of unliganded ribonuclease A (RNase A) and RNase A bou

SUBMITTER: Liu FC 

PROVIDER: S-EPMC12308374 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature