Backbone Assignment of Fully Protonated Solid Proteins by1H Detection and Ultrafast Magic-Angle-Spinning NMR Spectroscopy-Reference-Cited by-同舟云学术

Backbone Assignment of Fully Protonated Solid Proteins by1H Detection and Ultrafast Magic-Angle-Spinning NMR Spectroscopy

Published:2012-09-28 Issue:43 Volume:51 Page:10756-10759
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Marchetti Alessandro,Jehle Stefan,Felletti Michele,Knight Michael J.,Wang Yao,Xu Zhi-Qiang,Park Ah Young,Otting Gottfried,Lesage Anne,Emsley Lyndon,Dixon Nicholas E.,Pintacuda Guido

Publisher

Wiley

Subject

General Chemistry,Catalysis

Reference43 articles.

1. Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR

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

3. Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers

4. N-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneity

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