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Sequential Digestion with Trypsin and Elastase in Cross-Linking Mass Spectrometry

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)4472-4478
Number of pages7
JournalAnalytical Chemistry
Volume91
Issue number7
Early online date28 Feb 2019
DOIs
DateAccepted/In press - 28 Feb 2019
DateE-pub ahead of print - 28 Feb 2019
DatePublished (current) - 2 Apr 2019

Abstract

Cross-linking mass spectrometry has become an important approach for studying protein structures and protein-protein interactions. The amino acid compositions of some protein regions impede the detection of cross-linked residues, although it would yield invaluable information for protein modeling. Here, we report on a sequential-digestion strategy with trypsin and elastase to penetrate regions with a low density of trypsin-cleavage sites. We exploited intrinsic substrate-recognition properties of elastase to specifically target larger tryptic peptides. Our application of this protocol to the TAF4-12 complex allowed us to identify cross-links in previously inaccessible regions.

    Research areas

  • Synthetic biology

    Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

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    Rights statement: This is the final published version of the article (version of record). It first appeared online via ACS at https://doi.org/10.1021/acs.analchem.8b05222 . Please refer to any applicable terms of use of the publisher.

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    Licence: CC BY

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