Backbone Hydrogen Bond Strengths Can Vary Widely in Transmembrane Helices-Reference-Cited by-同舟云学术

Backbone Hydrogen Bond Strengths Can Vary Widely in Transmembrane Helices

Published:2017-07-10 Issue:31 Volume:139 Page:10742-10749
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cao Zheng¹,Hutchison James M.²,Sanders Charles R.²,Bowie James U.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, UCLA-DOE Institute, Molecular Biology Institute, University of California, Los Angeles, California 90095, United States

2. Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37240, United States

Funder

National Institute on Aging

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.7b04819

Reference97 articles.

1. Membrane protein folding: how important are hydrogen bonds?

2. Polar residues drive association of polyleucine transmembrane helices

3. Polar side chains drive the association of model transmembrane peptides

4. Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants

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