Microsecond Time Scale Mobility in a Solid Protein As Studied by the 15N R1ρ Site-Specific NMR Relaxation Rates-Reference-Cited by-同舟云学术

Microsecond Time Scale Mobility in a Solid Protein As Studied by the 15N R1ρ Site-Specific NMR Relaxation Rates

Published:2010-08-06 Issue:34 Volume:132 Page:11850-11853
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Krushelnitsky Alexey¹,Zinkevich Tatiana¹,Reichert Detlef¹,Chevelkov Veniamin¹,Reif Bernd¹

Affiliation:

1. Kazan Institute of Biochemistry and Biophysics, Kazan, Russia, Kazan Physical Technical Institute, Kazan, Russia, Institut für Physik - NMR, Martin-Luther-Universität Halle-Wittenberg, Halle, Germany, and Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja103582n

Reference17 articles.

1. Magic-Angle-Spinning Solid-State NMR Applied to Polypeptides and Proteins

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

3. Solid-state NMR and protein dynamics

4. Quantitative Analysis of Backbone Dynamics in a Crystalline Protein from Nitrogen-15 Spin−Lattice Relaxation

5. Measurement of N15-T1 relaxation rates in a perdeuterated protein by magic angle spinning solid-state nuclear magnetic resonance spectroscopy

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