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Protein Tertiary Structure by Crosslinking/Mass Spectrometry

Journal

TRENDS IN BIOCHEMICAL SCIENCES
Volume 43, Issue 3, Pages 157-169

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2017.12.006

Keywords

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Funding

  1. Wellcome Trust [103139, 108504, 203149]
  2. DFG [RA 2365/4-1]

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Observing the structures of proteins within the cell and tracking structural changes under different cellular conditions are the ultimate challenges for structural biology. This, however, requires an experimental technique that can generate sufficient data for structure determination and is applicable in the native environment of proteins. Crosslinking/mass spectrometry (CLMS) and protein structure determination have recently advanced to meet these requirements and crosslinking-driven de novo structure determination in native environments is now possible. In this opinion article, we highlight recent successes in the field of CLMS with protein structure modeling and challenges it still holds.

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