Transient Cross-linking Mass Spectrometry: Taking Conformational Snapshots of Proteins.

ABSTRACT: The dynamic nature of protein conformations is central to their biological functions. Conventional structural biology techniques provide static snapshots, whereas a comprehensive understanding requires an analysis of the dynamic conformations. In this study, we develop a transient cross-linking mass spectrometry method using a photo-cross-linker DCD. This cross-linker can be transiently activated to accomplish cross-linking, and with sample freezing, transient conformations are preserved, allowing temporal control and on-demand cross-linking. Its cross-linking site covers all amino acids, exhibiting diversity and providing rich structural information. Additionally, we develop a data-processing strategy by integrating a DCD-specific reporter ion and a defined ambiguous site annotation crite

SUBMITTER: Xie Y 

PROVIDER: S-EPMC11923955 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature