(Q28202979)

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15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings

scientific article (publication date: September 2003)

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15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings (English)

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Rebecca S Lipsitz

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Nico Tjandra

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2

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language of work or name

English

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publication date

September 2003

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published in

Journal of Magnetic Resonance

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volume

164

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issue

1

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page(s)

171-6

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cites work

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

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Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution

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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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Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein

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Prediction of proton chemical shifts in RNA. Their use in structure refinement and validation

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The impact of direct refinement against proton chemical shifts on protein structure determination by NMR.

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Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

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NMR structures of biomolecules using field oriented media and residual dipolar couplings

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Structure of Bax: coregulation of dimer formation and intracellular localization

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Carbonyl CSA restraints from solution NMR for protein structure refinement

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Simple multidimensional NMR experiments to obtain different types of one-bond dipolar couplings simultaneously.

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Measurement of Proton, Nitrogen, and Carbonyl Chemical Shielding Anisotropies in a Protein Dissolved in a Dilute Liquid Crystalline Phase

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Magnetic Field Dependence of Nitrogen−ProtonJSplittings in15N-Enriched Human Ubiquitin Resulting from Relaxation Interference and Residual Dipolar Coupling

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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The Xplor-NIH NMR molecular structure determination package

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Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach

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Orientation of amide-nitrogen-15 chemical shift tensors in peptides: a quantum chemical study.

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Identifiers

DOI

10.1016/S1090-7807(03)00176-9

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PubMed publication ID

12932470

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(Q28202979)

15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings

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