The '"C off-resonance rotating frame spin-lattice relaxation technique is applicable to the study of protein rotational diffusion behavior in both model in vitro and in vivo systems. The original formalism of James and co-workers [(1978) J. Am. Chem. SOC. 100, 3590-35941 was constrained by the assum
Assessment of protien reorientational diffusion in solution by 13C off-resonance rotating frame spin–lattice relaxation: Effect of anisotropic tumbling
✍ Scribed by Courtesy F. Morgan; Thomas Schlieich; G. Herbert Caines; David Michael
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1990
- Tongue
- English
- Weight
- 811 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
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.
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## Abstract Evidence is presented which shows that hemoglobin S in sickle cells has a tendency to aggregate even in the oxygenated state. The basis for that conclusion is derived from ^13^C‐nmr rotating‐frame spin–lattice relaxation studies in the presence of an off‐resonance radiofrequency field i