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 language | English (US) |
|---|---|
| Title of host publication | Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics |
| Pages | 267-268 |
| Number of pages | 2 |
| State | Published - 2002 |
| Externally published | Yes |
| Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Other
| Other | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
|---|---|
| Country | United States |
| City | Orlando, FL |
| Period | 6/2/02 → 6/6/02 |
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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)