Three-Dimensional Structure of the Water-Insoluble Protein Crambin in Dodecylphosphocholine Micelles and Its Minimal Solvent-Exposed Surface-Reference-Cited by-同舟云学术

Three-Dimensional Structure of the Water-Insoluble Protein Crambin in Dodecylphosphocholine Micelles and Its Minimal Solvent-Exposed Surface

Published:2006-03-09 Issue:13 Volume:128 Page:4398-4404
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ahn Hee-Chul¹,Juranić Nenad¹,Macura Slobodan¹,Markley John L.¹

Affiliation:

1. Contribution from the National Magnetic Resonance Facility at Madison, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, and Departments of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, Minnesota, 55905

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja057773d

Reference42 articles.

1. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

2. THE USE OF 2H, 13C, 15N MULTIDIMENSIONAL NMR GTO STUDY THE STRUCTURE AND DYNAMICS OF PROTEINS

3. Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles

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