Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains.

ABSTRACT: Disordered regions are an important functional feature of many multidomain proteins. A prime example is proteins in membraneless organelles, which contain folded domains that engage in specific interactions and disordered low-complexity (LC) domains that mediate liquid-liquid phase separation. Studying these complex architectures remains challenging due to their conformational variability. Native mass spectrometry (nMS) is routinely employed to analyze conformations and interactions of folded or disordered proteins; however, its ability to analyze proteins with disordered LC domains has not been investigated. Here, we analyze the ionization and conformational states of designed model proteins that recapitulate key features of proteins found in membraneless organelles. Our results show that

SUBMITTER: Osterholz H 

PROVIDER: S-EPMC11775691 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature