Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide 13CO to Lipid 31P Proximities Support Similar Partially Inserted Membrane Locations of the α Helical and β Sheet Peptide Structures-Reference-Cited by-同舟云学术

Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide 13CO to Lipid 31P Proximities Support Similar Partially Inserted Membrane Locations of the α Helical and β Sheet Peptide Structures

Published:2013-02-28 Issue:39 Volume:117 Page:9848-9859
ISSN:1089-5639
Container-title:The Journal of Physical Chemistry A
language:en
Short-container-title:J. Phys. Chem. A

Author:

Gabrys Charles M.¹,Qiang Wei¹,Sun Yan¹,Xie Li¹,Schmick Scott D.¹,Weliky David P.¹

Affiliation:

1. Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp312845w

Reference44 articles.

1. Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme

2. Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Human Immunodeficiency Virus gp41 Protein That Includes the Fusion Peptide: NMR Detection of Recombinant Fgp41 in Inclusion Bodies in Whole Bacterial Cells and Structural Characterization of Purified and Membrane-Associated Fgp41

3. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (Review)

4. Are fusion peptides a good model to study viral cell fusion?

5. Oligomeric β-Structure of the Membrane-Bound HIV-1 Fusion Peptide Formed from Soluble Monomers

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