𝔖 Bobbio Scriptorium
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Exploring the conformational space of Vpu from HIV-1: A versatile adaptable protein

✍ Scribed by Jens Krüger; Wolfgang B. Fischer

Book ID
102876943
Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
566 KB
Volume
29
Category
Article
ISSN
0192-8651

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✦ Synopsis

Abstract

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. © 2008 Wiley Periodicals, Inc. J Comput Chem 2008.

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