Stabilizing Proteins by Chemical Cross-Linking: Insights into Conformation, Unfolding, and Aggregation Using Native Ion Mobility Mass Spectrometry.

ABSTRACT: The function and stability of proteins depend on their three-dimensional structure, which includes conformational dynamics and potential self-assembly. Protein structural organization is particularly important in biotechnological applications, where protein integrity is often challenged by nonphysiological conditions, leading to disassembly, aggregation, and eventually the loss of function or activity. The use of chemical cross-linking strategies, such as the in situ cyclization of proteins (INCYPRO), can overcome these challenges, providing proteins and protein complexes with enhanced resistance to thermal and chemical stress. To probe how cross-linking affects protein structure and stability, we combined native ion mobility mass spectrometry (nIM-MS) and collision-induced unfolding (CIU)

SUBMITTER: Sadighi R 

PROVIDER: S-EPMC12676522 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature