Transverse-Dephasing Optimized Homonuclear J-Decoupling in Solid-State NMR Spectroscopy of Uniformly 13C-Labeled Proteins-Reference-Cited by-同舟云学术

Transverse-Dephasing Optimized Homonuclear J-Decoupling in Solid-State NMR Spectroscopy of Uniformly 13C-Labeled Proteins

Published:2009-07-15 Issue:31 Volume:131 Page:10816-10817
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Laage Ségolène¹,Lesage Anne¹,Emsley Lyndon¹,Bertini Ivano¹,Felli Isabella C.¹,Pierattelli Roberta¹,Pintacuda Guido¹

Affiliation:

1. Université de Lyon, CNRS/ ENS Lyon/ UCB-Lyon 1, Centre RMN à Très Hauts Champs, 5 rue de la Doua, 69100 Villeurbanne, France, and Department of Chemistry and Magnetic Resonance Center (CERM), University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja903542h

Reference21 articles.

1. Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward

2. Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

3. Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR

4. 3D Protein Structures by Solid-State NMR Spectroscopy: Ready for High Resolution

5. Constant-Time Through-Bond 13C Correlation Spectroscopy for Assigning Protein Resonances with Solid-State NMR Spectroscopy

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