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000055021 084__ $$2WoS$$aBiochemistry & Molecular Biology
000055021 084__ $$2WoS$$aBiophysics
000055021 1001_ $$0P:(DE-HGF)0$$aLemaitre, V.$$b0
000055021 245__ $$aFull length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy
000055021 260__ $$aGuilderland, NY$$bAdenine Press$$c2006
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000055021 440_0 $$016381$$aJournal of Biomolecular Structure & Dynamics$$v23$$x0739-1102
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000055021 520__ $$aBased on structures made available by solution NMR, molecular models of the protein Vpu from HIV-1 were built and refined by 6 ns MD simulations in a fully hydrated lipid bilayer. Vpu is an 81 amino acid type I integral membrane protein encoded by the human immunodeficiency virus type-1 (HIV- 1) and closely related simian immunodeficiency viruses (SIVs). Its role is to amplify viral release. Upon phosphorylation, the cytoplasmic domain adopts a more compact shape with helices 2 and 3 becoming almost parallel to each other. A loss of helicity for several residues belonging to the helices adjacent to both ends of the loop region containing serines 53 and 57 is observed. A fourth helix, present in one of: the NMR-based Structures of the cytoplasmic domain and located near the C-terminus, is lost upon phosphorylation.
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000055021 65320 $$2Author$$aVpu
000055021 65320 $$2Author$$aHIV-1
000055021 65320 $$2Author$$amembrane protein
000055021 65320 $$2Author$$amolecular dynamics simulations
000055021 65320 $$2Author$$aNMR spectroscopy
000055021 7001_ $$0P:(DE-HGF)0$$aWray, V.$$b1
000055021 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b2$$uFZJ
000055021 7001_ $$0P:(DE-HGF)0$$aWatts, A.$$b3
000055021 7001_ $$0P:(DE-HGF)0$$aFischer, W. B.$$b4
000055021 773__ $$0PERI:(DE-600)2085732-9$$gVol. 23, p. 485 - 496$$p485 - 496$$q23<485 - 496$$tJournal of biomolecular structure & dynamics$$v23$$x0739-1102$$y2006
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