Mapping contact surfaces in HIV-1 capsid protein hexamer by H/D exchange and on-line HPLC electrospray ionization fourier transform ion cyclotron resonance mass analysis

TuKiet T. Lam, Jason K. Lanman, Mark Emmett, Christopher L. Hendrickson, Peter E. Prevelige, Alan G. Marshall

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The mapping of contact surfaces in the monomer subunits by hydrogen/deuterium exchange and on-line HPLC electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) was discussed. The CA protein existed in monomer-dimer equilibrium at low salt concentration and polymerized into long tube-like structures at high ionic strength. Recombinant CA protein was expressed in E. coli, the cells were lysed and capsid proteins were precipitated with ammonium sulfate. The results show that FT-ICR MS produces high primary protein sequence coverage (∼90%).

Original languageEnglish (US)
Title of host publicationProceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages267-268
Number of pages2
StatePublished - 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

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ASJC Scopus subject areas

  • Spectroscopy

Cite this

Lam, T. T., Lanman, J. K., Emmett, M., Hendrickson, C. L., Prevelige, P. E., & Marshall, A. G. (2002). Mapping contact surfaces in HIV-1 capsid protein hexamer by H/D exchange and on-line HPLC electrospray ionization fourier transform ion cyclotron resonance mass analysis. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 267-268)