Comprehensive identification of disulfide bonds using non-specific proteinase K digestion and CID-cleavable crosslinking analysis methodology for Orbitrap LC/ESI-MS/MS data

Karl A.T. Makepeace, Jason J. Serpa, Evgeniy V. Petrotchenko, Christoph H. Borchers

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Disulfide bonds are valuable constraints in protein structure modeling. The Cys-Cys disulfide bond undergoes specific fragmentation under CID and, therefore, can be considered as a CID-cleavable crosslink. We have recently reported on the benefits of using non-specific digestion with proteinase K for inter-peptide crosslink determination. Here, we describe an updated application of our CID-cleavable crosslink analysis software and our crosslinking analysis with non-specific digestion methodology for the robust and comprehensive determination of disulfide bonds in proteins, using Orbitrap LC/ESI-MS/MS data.

Original languageEnglish
Pages (from-to)74-78
Number of pages5
JournalMethods
Volume89
DOIs
Publication statusPublished - 1 Nov 2015
Externally publishedYes

Keywords

  • Crosslinking
  • Disulfide
  • Mass spectrometry
  • Zero-length

Fingerprint

Dive into the research topics of 'Comprehensive identification of disulfide bonds using non-specific proteinase K digestion and CID-cleavable crosslinking analysis methodology for Orbitrap LC/ESI-MS/MS data'. Together they form a unique fingerprint.

Cite this