Fibrillarin:Nop5 complex binding surfaces mapped by H/D exchange and LC micro-electrospray ionization fourier transform ion cyclotron resonance mass analysis

Fangmin Xu, Tu Kiet T. Lam, Mark R. Emmett, Christopher L. Hendrickson, Hong Li, Alan G. Marshall

Research output: Contribution to conferencePaper

Abstract

The mapping of the complex binding surfaces of small nucleolar ribonucleoproteins (snoRNP), fibrillarin and Nop5, was presented. The solution-phase hydrogen/deuterium exchange (HDX) was combined with liquid chromatography (LC) microelectrospray ionization Fourier transform ion cyclotron resonance mass analysis (ESI FT-ICR MS) for the mapping. Metal affinity chromatography and dialysis were used to purify the the complex protein before the HDX was performed. A decrease in HDX rate for peptic fragment 70-80 of fibrillarin was observed when fibrillarin formed a complex with Nop5.

Original languageEnglish (US)
Pages299-300
Number of pages2
StatePublished - Dec 1 2002
Externally publishedYes
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

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

ASJC Scopus subject areas

  • Spectroscopy

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    Xu, F., Lam, T. K. T., Emmett, M. R., Hendrickson, C. L., Li, H., & Marshall, A. G. (2002). Fibrillarin:Nop5 complex binding surfaces mapped by H/D exchange and LC micro-electrospray ionization fourier transform ion cyclotron resonance mass analysis. 299-300. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.