% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Lemaitre:55021,
author = {Lemaitre, V. and Wray, V. and Willbold, D. and Watts, A.
and Fischer, W. B.},
title = {{F}ull length {V}pu from {HIV}-1: {C}ombining molecular
dynamics simulations with {NMR} spectroscopy},
journal = {Journal of biomolecular structure $\&$ dynamics},
volume = {23},
issn = {0739-1102},
address = {Guilderland, NY},
publisher = {Adenine Press},
reportid = {PreJuSER-55021},
pages = {485 - 496},
year = {2006},
note = {Record converted from VDB: 12.11.2012},
abstract = {Based 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.},
keywords = {J (WoSType)},
cin = {IBI-2 / JARA-SIM},
ddc = {570},
cid = {I:(DE-Juel1)VDB58 / I:(DE-Juel1)VDB1045},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biochemistry $\&$ Molecular Biology / Biophysics},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000236290300001},
url = {https://juser.fz-juelich.de/record/55021},
}