Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation-Reference-Cited by-同舟云学术

Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation

Published:2011-08-22 Issue:36 Volume:133 Page:14184-14187
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lorieau Justin L.¹,Louis John M.¹,Bax Ad¹

Affiliation:

1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, United States

Funder

National Institute of Diabetes and Digestive and Kidney Diseases

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja2045309

Reference42 articles.

1. THE STRUCTURE AND FUNCTION OF THE HEMAGGLUTININ MEMBRANE GLYCOPROTEIN OF INFLUENZA VIRUS

2. Influenza hemagglutinin is spring-loaded by a metastable native conformation

3. Composition and Functions of the Influenza Fusion Peptide

4. Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2.

5. The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface

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