Using homobifunctional crosslinking reagents with normal and N-15 labeled proteins for the determination of protein tertiary structure and protein-protein interactions

Xin Guo, Birgit Schilling, Malin Young, Matyas Medzihradszky, Irwin D. Kuntz, R. Kip Guy, Bradford W. Gibson

Research output: Contribution to conferencePaperpeer-review

4 Scopus citations

Abstract

The determination of protein structure and protein-protein interactions using homobifunctional crosslinking reagents with normal and N-15 labeled proteins was discussed. Recombinant CMP-NeuAc synthetase and HIV-integrase were prepared from normal and N-15 enriched media. In the case of crosslinked peptides originating from protein-protein interactions, some gain was obtained from a pattern recognition point of view, since these peptide types were observed as quartets. The identification of crosslinked peptides was confirmed by electrospray ionization (ESI)-mass spectrometry (MS)/MS using a quadrupole time-of-flight (TOF) instrument or MALDI-PSD.

Original languageEnglish
Pages249-250
Number of pages2
StatePublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Conference

ConferenceProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/TerritoryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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