dc.contributor.author | Kukol, A. | |
dc.contributor.author | Arkin, I.T. | |
dc.date.accessioned | 2011-10-18T10:01:10Z | |
dc.date.available | 2011-10-18T10:01:10Z | |
dc.date.issued | 1999-09 | |
dc.identifier.citation | Kukol , A & Arkin , I T 1999 , ' Vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching ' , Biophysical Journal , vol. 77 , no. 3 , pp. 1594-1601 . https://doi.org/10.1016/S0006-3495(99)77007-4 | |
dc.identifier.issn | 0006-3495 | |
dc.identifier.uri | http://hdl.handle.net/2299/6692 | |
dc.description | Full text of this article is not available in the UHRA | |
dc.description.abstract | The recently developed method of site-directed Fourier transform infrared dichroism for obtaining orientational constraints of oriented polymers is applied here to the transmembrane domain of the vpu protein from the human immunodeficiency virus type 1 (HIV-1). The infrared spectra of the 31-residue-long vpu peptide reconstituted in lipid vesicles reveal a predominantly alpha-helical structure. The infrared dichroism data of the C-13-labeled peptide yielded a helix tilt beta = (6.5 +/- 1.7)degrees from the membrane normal. The rotational pitch angle omega, defined as zero for a residue located in the direction of the helix tilt, is omega = (283 +/- 11)degrees for the C-13 labels Va(13)/Val(20) and omega = (23 +/- 11)degrees for the C-13 labels Ala(14)/Val(21). A global molecular dynamics search protocol restraining the helix tilt to the experimental value was performed for oligomers of four, five, and six subunits. From 288 structures for each oligomer, a left-handed pentameric coiled coil was obtained, which best fits the experimental data. The structure reveals a pore occluded by Trp residues at the intracellular end of the transmembrane domain. | en |
dc.format.extent | 8 | |
dc.language.iso | eng | |
dc.relation.ispartof | Biophysical Journal | |
dc.subject | IMMUNODEFICIENCY-VIRUS TYPE-1 | |
dc.subject | ION CHANNELS | |
dc.subject | CONFORMATIONAL-CHANGES | |
dc.subject | SECONDARY STRUCTURE | |
dc.subject | MEMBRANE-PROTEIN | |
dc.subject | RELEASE | |
dc.subject | GENE | |
dc.subject | BACTERIORHODOPSIN | |
dc.subject | PHOSPHORYLATION | |
dc.subject | IDENTIFICATION | |
dc.title | Vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching | 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/S0006-3495(99)77007-4 | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |