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

Tu Kiet T. Lam; Jason K. Lanman; Mark R. Emmett; Christopher L. Hendrickson; Peter E. Prevelige; Alan G. Marshall

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

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

Research output: Contribution to conference › Paper › peer-review

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)
Pages	267-268
Number of pages	2
State	Published - Dec 1 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

ASJC Scopus subject areas

Spectroscopy

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Lam, T. K. T., Lanman, J. K., Emmett, M. R., 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. 267-268. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

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. / Lam, Tu Kiet T.; Lanman, Jason K.; Emmett, Mark R.; Hendrickson, Christopher L.; Prevelige, Peter E.; Marshall, Alan G.

2002. 267-268 Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Research output: Contribution to conference › Paper › peer-review

Lam, TKT, Lanman, JK, Emmett, MR, Hendrickson, CL, Prevelige, PE & Marshall, AG 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', Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States, 6/2/02 - 6/6/02 pp. 267-268.

Lam TKT, Lanman JK, Emmett MR, Hendrickson CL, Prevelige PE, Marshall AG. 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. 2002. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Lam, Tu Kiet T. ; Lanman, Jason K. ; Emmett, Mark R. ; Hendrickson, Christopher L. ; Prevelige, Peter E. ; Marshall, Alan G. / 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. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.2 p.

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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%).",

author = "Lam, {Tu Kiet T.} and Lanman, {Jason K.} and Emmett, {Mark R.} and Hendrickson, {Christopher L.} and Prevelige, {Peter E.} and Marshall, {Alan G.}",

year = "2002",

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language = "English (US)",

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AU - Hendrickson, Christopher L.

AU - Prevelige, Peter E.

AU - Marshall, Alan G.

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N2 - 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%).

AB - 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%).

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