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

Jens Krüger, Wolfgang B. Fischer

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

The dynamic behavior of monomeric Vpu1-32 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.

Original languageEnglish
Pages (from-to)2416-2424
Number of pages9
JournalJournal of Computational Chemistry
Volume29
Issue number14
DOIs
StatePublished - 15 Nov 2008

Keywords

  • HIV-1
  • Lipid bilayers
  • MD simulations
  • Membrane proteins
  • Protein stability
  • Vpu

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