| pubmed-article:10465770 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C0597196 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C0596957 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C0596436 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C1301820 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C0282183 | lld:lifeskim |
| pubmed-article:10465770 | lifeskim:mentions | umls-concept:C2348867 | lld:lifeskim |
| pubmed-article:10465770 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10465770 | pubmed:dateCreated | 1999-10-8 | lld:pubmed |
| pubmed-article:10465770 | pubmed:abstractText | 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 (13)C-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 (13)C labels Val(13)/Val(20) and omega = (23 +/- 11) degrees for the (13)C 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. | lld:pubmed |
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| pubmed-article:10465770 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10465770 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10465770 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10465770 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10465770 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10465770 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:10465770 | pubmed:author | pubmed-author:ArkinI TIT | lld:pubmed |
| pubmed-article:10465770 | pubmed:author | pubmed-author:KukolAA | lld:pubmed |
| pubmed-article:10465770 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10465770 | pubmed:volume | 77 | lld:pubmed |
| pubmed-article:10465770 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10465770 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10465770 | pubmed:pagination | 1594-601 | lld:pubmed |
| pubmed-article:10465770 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10465770 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10465770 | pubmed:articleTitle | vpu transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching. | lld:pubmed |
| pubmed-article:10465770 | pubmed:affiliation | Cambridge Center for Molecular Recognition, Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, England. | lld:pubmed |
| pubmed-article:10465770 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10465770 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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