(Q57101061)

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Measurement of 15N chemical shift anisotropy in a protein dissolved in a dilute liquid crystalline medium with the application of magic angle sample spinning

scientific article published on 01 July 2003

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5 November 2019

Measurement of 15N chemical shift anisotropy in a protein dissolved in a dilute liquid crystalline medium with the application of magic angle sample spinning (English)

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5 November 2019

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Jun-ichi Kurita

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5 November 2019

Hideto Shimahara

2

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5 November 2019

Naoko Utsunomiya-Tate

3

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5 November 2019

Shin-ichi Tate

4

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5 November 2019

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1 July 2003

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5 November 2019

Journal of Magnetic Resonance

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5 November 2019

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5 November 2019

1

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5 November 2019

163-173

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5 November 2019

Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

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The effect of noncollinearity of 15N-1H dipolar and 15N CSA tensors and rotational anisotropy on 15N relaxation, CSA/dipolar cross correlation, and TROSY.

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Effects of Dynamics and Environment on15N Chemical Shielding Anisotropy in Proteins. A Combination of Density Functional Theory, Molecular Dynamics Simulation, and NMR Relaxation

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Measurement of cross correlation between dipolar coupling and chemical shift anisotropy in the spin relaxation of 13C, 15N-labeled proteins

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Cross-correlated relaxation for measurement of angles between tensorial interactions.

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A simple one-dimensional solid-state NMR method to characterize the nuclear spin interaction tensors associated with the peptide bond.

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Characterization of15N Chemical Shift and1H−15N Dipolar Coupling Interactions in a Peptide Bond of Uniaxially Oriented and Polycrystalline Samples by One-Dimensional Dipolar Chemical Shift Solid-State NMR Spectroscopy

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Experimental aspects of multidimensional solid-state NMR correlation spectroscopy

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Model-Independent Analysis of15N Chemical Shift Anisotropy from NMR Relaxation Data. Ubiquitin as a Test Example

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An Approach to Direct Determination of Protein Dynamics from15N NMR Relaxation at Multiple Fields, Independent of Variable15N Chemical Shift Anisotropy and Chemical Exchange Contributions

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Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy.

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Protein Backbone Dynamics and 15 N Chemical Shift Anisotropy from Quantitative Measurement of Relaxation Interference Effects

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Sign determination of dipolar couplings in field-oriented bicelles by variable angle sample spinning (VASS)

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Manipulation of the director in bicellar mesophases by sample spinning: a new tool for NMR spectroscopy.

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Evaluation of uncertainty in alignment tensors obtained from dipolar couplings

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High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium

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Dipolar couplings in macromolecular structure determination

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Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules

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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

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Order matrix analysis of residual dipolar couplings using singular value decomposition.

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Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements

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Fast internal main-chain dynamics of human ubiquitin

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Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules

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Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values

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Identifiers

10.1016/S1090-7807(03)00080-6

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