dc.contributor.author | Cordes, F. S. | |
dc.contributor.author | Kukol, A. | |
dc.contributor.author | Forrest, L. R. | |
dc.contributor.author | Arkin, I.T. | |
dc.contributor.author | Sansom, M. S. P. | |
dc.contributor.author | Fischer, W. B. | |
dc.date.accessioned | 2011-10-18T10:01:15Z | |
dc.date.available | 2011-10-18T10:01:15Z | |
dc.date.issued | 2001-06-06 | |
dc.identifier.citation | Cordes , F S , Kukol , A , Forrest , L R , Arkin , I T , Sansom , M S P & Fischer , W B 2001 , ' The structure of the HIV-1 Vpu ion channel: modelling and simulation studies ' , Biochimica et Biophysica Acta - Biomembranes , vol. 1512 , no. 2 , pp. 291-298 . https://doi.org/10.1016/S0005-2736(01)00332-7 | |
dc.identifier.issn | 0005-2736 | |
dc.identifier.uri | http://hdl.handle.net/2299/6697 | |
dc.description.abstract | Vpu is an 81 amino acid auxiliary protein in HIV-1 which exhibits channel activity. We used two homo-pentameric bundles with the helical transmembrane segments derived from FTIR spectroscopy in combination with a global molecular dynamics search protocol: (i) tryptophans (W) pointing into the pore, and (ii) W facing the lipids. Two equivalent bundles have been generated using a simulated annealing via a restrained molecular dynamics simulations (SA/MD) protocol. A fifth model was generated via SA/MD with all serines facing the pore. The latter model adopts a very stable structure during the 2 ns of simulation. The stability of the models with W facing the pore depends on the starting structure. A possible gating mechanism is outlined. (C) 2001 Elsevier Science B.V. All rights reserved. | en |
dc.format.extent | 8 | |
dc.language.iso | eng | |
dc.relation.ispartof | Biochimica et Biophysica Acta - Biomembranes | |
dc.subject | HIV-1 | |
dc.subject | Vpu | |
dc.subject | viral ion channel | |
dc.subject | molecular dynamics | |
dc.subject | gating | |
dc.subject | INFLUENZA-A VIRUS | |
dc.subject | SOLID-STATE NMR | |
dc.subject | MOLECULAR-DYNAMICS SIMULATIONS | |
dc.subject | TRANSMEMBRANE DOMAIN | |
dc.subject | M2 CHANNEL | |
dc.subject | ACETYLCHOLINE-RECEPTOR | |
dc.subject | CYTOPLASMIC DOMAIN | |
dc.subject | GRAMICIDIN CHANNEL | |
dc.subject | INFRARED DICHROISM | |
dc.subject | MEMBRANE-PROTEIN | |
dc.title | The structure of the HIV-1 Vpu ion channel: modelling and simulation studies | en |
dc.contributor.institution | School of Life and Medical Sciences | |
dc.contributor.institution | Biosciences Research Group | |
dc.contributor.institution | Centre for Research in Mechanisms of Disease and Drug Discovery | |
dc.contributor.institution | Department of Clinical, Pharmaceutical and Biological Science | |
dc.contributor.institution | Centre for Future Societies Research | |
dc.description.status | Peer reviewed | |
rioxxterms.versionofrecord | 10.1016/S0005-2736(01)00332-7 | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |