Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein-Reference-Cited by-同舟云学术

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Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein

Published:2017-06-30 Issue:27 Volume:139 Page:9246-9258
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Good Daryl,Pham Charlie,Jagas Jacob,Lewandowski Józef R.¹,Ladizhansky Vladimir^ORCID

Affiliation:

1. Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom

Funder

Canada Foundation for Innovation

Bill and Melinda Gates Foundation

FP7 Ideas: European Research Council

Natural Sciences and Engineering Research Council of Canada

Biotechnology and Biological Sciences Research Council

Ministry of Research and Innovation

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.7b03974

Reference82 articles.

1. Dynamic personalities of proteins

2. Packing defects, cavities, volume fluctuations, and access to the interior of proteins. Including some general comments on surface area and protein structure

3. Protein dynamics and function from solution state NMR spectroscopy

4. Solution NMR Spectroscopy for the Study of Enzyme Allostery

5. Characterization of the Dynamics of Biomacromolecules Using Rotating-Frame Spin Relaxation NMR Spectroscopy

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