Nuclear magnetic resonance (NMR) spectroscopy has been used to put in place the final piece of the HIV-1 protein structure, the cytoplasmic tail of gp41 protein. The research by a team at the University of Alabama at Birmingham led by Jamil Saad will help scientists better understand how the virus infects human cells and how progeny viruses are assembled and released from infected cells.
Mobility and Core-Protein Binding Patterns of DisorderedC-Terminal Tails in ?-Tubulin Isotypes
Mobility and Core-Protein Binding Patterns of DisorderedC-Terminal Tails in ?-Tubulin Isotypes
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Biochemistry
DOI: 10.1021/acs.biochem.6b00988
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NMR structure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins.
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FEBS J. 2015 Jan;282(2):341-60
Authors: Carbajo RJ, Sanz L, Perez A, Calvete JJ
Abstract
Extant disintegrins, as found in the venoms of Viperidae and...
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[NMR paper] Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
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J Mol Biol. 2013 Nov 15;
Authors: Sackett K, Nethercott MJ, Zheng Z, Weliky DP
Abstract
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although...
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Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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