Multiple Locations of Peptides in the Hydrocarbon Core of Gel-Phase Membranes Revealed by Peptide 13C to Lipid 2H Rotational-Echo Double-Resonance Solid-State Nuclear Magnetic Resonance
Author:
Affiliation:
1. Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States
Funder
National Institute of Allergy and Infectious Diseases
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi501211x
Reference32 articles.
1. A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide
2. 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
3. Interactions of the HIV-1 fusion peptide with large unilamellar vesicles and monolayers. A cryo-TEM and spectroscopic study
4. Membrane Protein Topology Probed by 1H Spin Diffusion from Lipids Using Solid-State NMR Spectroscopy
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. 2H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pH;Biochimica et Biophysica Acta (BBA) - Biomembranes;2020-10
2. Concepts and Methods of Solid-State NMR Spectroscopy Applied to Biomembranes;Chemical Reviews;2017-09-14
3. REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins;Journal of Magnetic Resonance;2015-04
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