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) |
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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 |
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Country | United States |
City | Orlando, FL |
Period | 6/2/02 → 6/6/02 |
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ASJC Scopus subject areas
- Spectroscopy
Cite this
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, TuKiet T.; Lanman, Jason K.; Emmett, Mark; Hendrickson, Christopher L.; Prevelige, Peter E.; Marshall, Alan G.
Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics. 2002. p. 267-268.Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
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TY - GEN
T1 - 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
AU - Lam, TuKiet T.
AU - Lanman, Jason K.
AU - Emmett, Mark
AU - Hendrickson, Christopher L.
AU - Prevelige, Peter E.
AU - Marshall, Alan G.
PY - 2002
Y1 - 2002
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%).
UR - http://www.scopus.com/inward/record.url?scp=2442716717&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=2442716717&partnerID=8YFLogxK
M3 - Conference contribution
AN - SCOPUS:2442716717
SP - 267
EP - 268
BT - Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
ER -