High Resolution 1H-Detected Solid-State NMR Spectroscopy of Protein Aliphatic Resonances: Access to Tertiary Structure Information-Reference-Cited by-同舟云学术

High Resolution 1H-Detected Solid-State NMR Spectroscopy of Protein Aliphatic Resonances: Access to Tertiary Structure Information

Published:2010-10-12 Issue:43 Volume:132 Page:15133-15135
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Asami Sam¹,Schmieder Peter¹,Reif Bernd¹

Affiliation:

1. Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Roessle-Str. 10, 13125 Berlin, Germany, Technische Universität München, Department of Chemistry, Lichtenbergstr. 4, 85747 Garching, Germany, and Helmholtz-Zentrum München (HMGU), Ingolstädter Landstr. 1, 85764 Neuherberg, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja106170h

Reference27 articles.

1. Long-Range Correlations between Aliphatic13C Nuclei in Protein MAS NMR Spectroscopy

2. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

3. General structural motifs of amyloid protofilaments

4. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril

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

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