Determinations of [N.sup.15] chemical shift anisotropy magnitudes in a uniformly [N.sup.15], [C.sup.13]-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy

Article Abstract:

A systematic study of the majority of [N.sup.15] amide chemical shift anisotropy (CSA) tensors in a microcrystalline protein of known structure is presented. The availability of previous high-resolution crystal and solution NMR structures will enhance the value of these measurements as a benchmark for the development of ab initio calculations of amide [N.sup.15] shielding tensor magnitudes.

Anisotropy, Amides, Chemical properties

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Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction

Article Abstract:

The potential capability of magic-angle spinning (MAs) solid-state NMR (SSNMR) to study the formulation chemistry of industrial and therapeutic proteins is demonstrated. The method could also be utilized to understand the phenomenon of single-crystal growth of proteins.

Observations, X-rays, X-ray diffraction, Spectra, Optical properties, Bacterial proteins, Crystallization

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Methyl dynamics in proteins from NMR slowly relaxing local structure spin relaxation analysis: A new perspective

Article Abstract:

NMR spin relaxation of [.sup.2.H] nuclei in [.sup.13.CH2]D groups is a powerful method for studying side-chain motion in proteins. The analysis is typically conducted with the original model-free (MF) approach adapted to methyl dynamics.

Methyl groups, Methyl compounds

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