Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins.
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.
Lewandowski
Józef R
JR
Université de Lyon, CNRS/ENS-Lyon/UCB-Lyon 1, Centre de RMN à Très Hauts Champs, 69100 Villeurbanne, France.
Sein
Julien
J
Blackledge
Martin
M
Emsley
Lyndon
L
D016880:Anisotropy; D003460:Crystallization; D008958:Models, Molecular; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins