Orientational and Motional Narrowing of Solid-State NMR Lineshapes of Uniaxially Aligned Membrane Proteins
Author:
Affiliation:
1. Department of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, North Carolina 27695-8240, United States
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp2092847
Reference45 articles.
1. High-Resolution Solid-State NMR Spectra of Integral Membrane Proteins Reconstituted into Magnetically Oriented Phospholipid Bilayers
2. Structural Evaluation of Phospholipid Bicelles for Solution-State Studies of Membrane-Associated Biomolecules
3. High-Resolution NMR Spectroscopy of Membrane Proteins in Aligned Bicelles
4. Structure Determination of a Membrane Protein with Two Trans-membrane Helices in Aligned Phospholipid Bicelles by Solid-State NMR Spectroscopy
5. Three-Dimensional Structure of the Transmembrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles
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