Deriving distance restraints from surface modified peptides in chemical crosslinking-mass spectrometry (CXMS) experiments

摘要

Quantitative CXMS data has the potential to elucidate conformational changesof proteins and protein complexes. Challenges exist to directly infer distance information from quantitative CXMS data, because changes in bothresidue reactivity and proximitywill have an impact on the amount of cross-linked peptides. Using heat shock protein 90 (Hsp90) as a model system, we explore various normalization schemes and modelsto eliminate the impact of the reactivity of cross-linked residues so that distance information can be inferred from quantitative CXMS data. Additionally, our study on the interaction of Hsp90 and a model client protein indicates a direct conformational coupling between Hsp90 and its client proteins.