Protein structure dynamics by crosslinking mass spectrometry

Zhuo Angel Chen, Juri Rappsilber*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract / Description of output

Crosslinking mass spectrometry captures protein structures in solution. The crosslinks reveal spatial proximities as distance restraints, but do not easily reveal which of these restraints derive from the same protein conformation. This superposition can be reduced by photo-crosslinking, and adding information from protein structure models, or quantitative crosslinking reveals conformation-specific crosslinks. As a consequence, crosslinking MS has proven useful already in the context of multiple dynamic protein systems. We foresee a breakthrough in the resolution and scale of studying protein dynamics when crosslinks are used to guide deep-learning-based protein modelling. Advances in crosslinking MS, such as photoactivatable crosslinking and in-situ crosslinking, will then reveal protein conformation dynamics in the cellular context, at a pseudo-atomic resolution, and plausibly in a time-resolved manner.

Original languageEnglish
Article number102599
JournalCurrent opinion in structural biology
Publication statusPublished - 1 Jun 2023

Keywords / Materials (for Non-textual outputs)

  • crosslinking mass spectrometry
  • photoactivatable crosslinking
  • protein conformational dynamics
  • protein structure modelling and prediction
  • quantitative analysis


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