Mapping native disulfide bonds at a proteome scale

Nat Methods. 2015 Apr;12(4):329-31. doi: 10.1038/nmeth.3283. Epub 2015 Feb 9.

Abstract

We developed a high-throughput mass spectrometry method, pLink-SS (http://pfind.ict.ac.cn/software/pLink/2014/pLink-SS.html), for precise identification of disulfide-linked peptides. Using pLink-SS, we mapped all native disulfide bonds of a monoclonal antibody and ten standard proteins. We performed disulfide proteome analyses and identified 199 disulfide bonds in Escherichia coli and 568 in proteins secreted by human endothelial cells. We discovered many regulatory disulfide bonds involving catalytic or metal-binding cysteine residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Disulfides / chemistry*
  • Escherichia coli / chemistry
  • Humans
  • Mass Spectrometry*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Library
  • Proteome / chemistry*
  • Proteomics / methods*
  • Ribonucleases / chemistry

Substances

  • Disulfides
  • Peptide Library
  • Proteome
  • Ribonucleases