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Assessment of protien reorientational diffusion in solution by 13 C off‐resonance rotating frame spin–lattice relaxation: Effect of anisotropic tumbling
Author(s) -
Morgan Courtesy F.,
Schlieich Thomas,
Caines G. Herbert,
Michael David
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360290302
Subject(s) - chemistry , anisotropy , spin diffusion , relaxation (psychology) , spin–lattice relaxation , diffusion , lattice (music) , nuclear magnetic resonance , resonance (particle physics) , frame (networking) , condensed matter physics , thermodynamics , atomic physics , physics , quantum mechanics , psychology , social psychology , nuclear quadrupole resonance , acoustics , telecommunications , computer science
The 13 C off‐resonance rotating frame spin‐lattice relaxation technique is applicable to the study of protien rotational diffusion behaviour in a variety of experimental situations. The original formalism of James and co‐workers (1978) ( J. Amer. Chem. Soc. 100 , 3590–3594) was constrained by the assumption of random isotropic reorientational motion. Here we include in the formalism anisotropic tumbling, and present the results of computer simulations illustrating the differences between anisotropic and isotropic reorientational motion for the off‐resonance rotating frame spin–lattice relaxation experiment. In addition, We have included chemical shift anisotropy of the peptide carbonyl carbon as an additional relaxation mechanism contribution, to permit high field nmr protein rotational diffusion measurements.