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231223s2008 xx |||||o 00| ||eng c |
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|a 10.1002/jcc.20986
|2 doi
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|a pubmed24n0597.xml
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|a (DE-627)NLM179119648
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|a (NLM)18432615
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Krüger, Jens
|e verfasserin
|4 aut
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|a Exploring the conformational space of Vpu from HIV-1
|b a versatile adaptable protein
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 03.12.2008
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|a Date Revised 07.10.2008
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|a published: Print
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|a Citation Status MEDLINE
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|a 2008 Wiley Periodicals, Inc.
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|a 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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|a Comparative Study
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Human Immunodeficiency Virus Proteins
|2 NLM
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|a Lipids
|2 NLM
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|a Viral Regulatory and Accessory Proteins
|2 NLM
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|a vpu protein, Human immunodeficiency virus 1
|2 NLM
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|a Fischer, Wolfgang B
|e verfasserin
|4 aut
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773 |
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|i Enthalten in
|t Journal of computational chemistry
|d 1984
|g 29(2008), 14 vom: 15. Nov., Seite 2416-24
|w (DE-627)NLM098138448
|x 1096-987X
|7 nnns
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773 |
1 |
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|g volume:29
|g year:2008
|g number:14
|g day:15
|g month:11
|g pages:2416-24
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|u http://dx.doi.org/10.1002/jcc.20986
|3 Volltext
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|a GBV_ILN_350
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|a AR
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|d 29
|j 2008
|e 14
|b 15
|c 11
|h 2416-24
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