Exploring the conformational space of Vpu from HIV-1 : a versatile adaptable protein
2008 Wiley Periodicals, Inc.
| Veröffentlicht in: | Journal of computational chemistry. - 1984. - 29(2008), 14 vom: 15. Nov., Seite 2416-24 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
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2008
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| Zugriff auf das übergeordnete Werk: | Journal of computational chemistry |
| Schlagworte: | Comparative Study Journal Article Research Support, Non-U.S. Gov't Human Immunodeficiency Virus Proteins Lipids Viral Regulatory and Accessory Proteins vpu protein, Human immunodeficiency virus 1 |
| Zusammenfassung: | 2008 Wiley Periodicals, Inc. The dynamic behavior of monomeric Vpu(1-32) from HIV-1 in different lipid environments has been studied. The peptide shows highly flexible behavior during the simulations and easily adapts to changing lipid environments as it experiences when travelling through the Golgi apparatus. Protein-lipid interactions do not show any significant correlation towards lipid type or thickness based on multiple 10 ns simulations. The averaged structure of a series of 16 independent simulations suggest kink around Ser-24, which compensates the polarity of its side chain by forming hydrogen bonds with the carbonyl backbone of adjacent amino acids towards the N-terminus |
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| Beschreibung: | Date Completed 03.12.2008 Date Revised 07.10.2008 published: Print Citation Status MEDLINE |
| ISSN: | 1096-987X |
| DOI: | 10.1002/jcc.20986 |