Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins

Journal of the American Chemical Society
Józef R LewandowskiLyndon Emsley

Abstract

A model for calculating the influence of anisotropic collective motions on NMR relaxation rates in crystalline proteins is presented. We show that small-amplitude (<10 degrees ) fluctuations may lead to substantial contributions to the (15)N spin-lattice relaxation rates and propose that the effect of domain motions should be included in solid-state NMR analyses of protein dynamics.

Citations

May 21, 2013·Progress in Biophysics and Molecular Biology·Yury E Shapiro
Apr 30, 2013·Accounts of Chemical Research·Józef Romuald Lewandowski
Jun 12, 2013·Accounts of Chemical Research·Sam Asami, Bernd Reif
Jul 20, 2011·Journal of the American Chemical Society·Józef R LewandowskiRobert G Griffin
Jun 23, 2012·Proceedings of the National Academy of Sciences of the United States of America·Michael J KnightGuido Pintacuda
Jun 30, 2011·BMC Bioinformatics·Michael T ZimmermannRobert L Jernigan
Jan 24, 2014·Protein Science : a Publication of the Protein Society·Yi Xue, Nikolai R Skrynnikov
May 2, 2015·Science·Józef R LewandowskiLyndon Emsley
Jan 17, 2015·The Journal of Physical Chemistry. B·Eva MeirovitchJack H Freed
Aug 8, 2014·Journal of the American Chemical Society·Emeline Barbet-MassinGuido Pintacuda
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Oct 6, 2015·Nature Communications·Peixiang MaPaul Schanda
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Aug 2, 2016·Angewandte Chemie·Jonathan M LamleyJózef R Lewandowski
Nov 6, 2015·Angewandte Chemie·Jonathan M LamleyJózef R Lewandowski
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