Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain.

  title={Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain.},
  author={Christopher P Jaroniec and Joshua D. Kaufman and Stephen J. Stahl and Mathias Viard and Robert Blumenthal and Paul T Wingfield and Adriaan Bax},
  volume={44 49},
The N-terminal fusion domain of the HIV-1 gp41 envelope glycoprotein is responsible for initiating the fusion of viral and cellular membranes, leading to the subsequent infection of the host cell by HIV-1. We have investigated the backbone structure and dynamics of the 30 N-terminal residues of HIV-1 gp41 in membrane-mimicking environments using NMR spectroscopy and (15)N- and (15)N,(13)C,(2)H-labeled peptides. Similar (15)N-(1)H HSQC spectra were obtained in a variety of detergents, including… CONTINUE READING

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Two - dimensional NMR methods for determining χ 1 angles of aromatic residues in proteins from three - bond JC ' C γ and JNC γ couplings

  • J. S. Hu, S. Grzesiek, A. Bax
  • J . Am . Chem . Soc .
  • 1997

A suite of triple resonance NMR experiments for the backbone assignment of 15 N , 13 C , 2 H labeled proteins with high sensitivity

  • T. Yamazaki, W. Lee, C. H. Arrowsmith, D. R. Muhandiram, L. E. Kay
  • J . Am . Chem . Soc .
  • 1994

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