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

Producción científica: Paperrevisión exhaustiva

4 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas249-250
Número de páginas2
EstadoPublished - 2002
EventoProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duración: jun 2 2002jun 6 2002

Conference

ConferenceProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
País/TerritorioUnited States
CiudadOrlando, FL
Período6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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