The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy (Q34042376)

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English	The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy	scientific article

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scholarly article

1 reference

Europe PubMed Central

30 July 2017

The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy (English)

1 reference

Europe PubMed Central

30 July 2017

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NMR spectroscopy

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Alexander Grishaev

object named as

Alexander Grishaev

2

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object named as

Lishan Yao

1

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Gabriel Cornilescu

object named as

Gabriel Cornilescu

3

0 references

4

object named as

Ad Bax

1 reference

Europe PubMed Central

30 July 2017

language of work or name

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publication date

1 August 2010

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Europe PubMed Central

30 July 2017

Journal of the American Chemical Society

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Europe PubMed Central

30 July 2017

132

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Europe PubMed Central

30 July 2017

31

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Europe PubMed Central

30 July 2017

10866-10875

1 reference

Europe PubMed Central

30 July 2017

Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements

1 reference

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Quantum-mechanics-derived 13Calpha chemical shift server (CheShift) for protein structure validation

1 reference

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1 reference

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Utilizing the charge field effect on amide (15)N chemical shifts for protein structure validation.

1 reference

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NMR determination of amide N-H equilibrium bond length from concerted dipolar coupling measurements.

1 reference

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Density functional calculations of 15N chemical shifts in solvated dipeptides.

1 reference

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Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.

1 reference

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Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology

1 reference

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A new model for chemical shifts of amide hydrogens in proteins

1 reference

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1 reference

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

1 reference

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Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G.

1 reference

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1 reference

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1 reference

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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.

1 reference

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

1 reference

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Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation

1 reference

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The use of chemical shifts and their anisotropies in biomolecular structure determination

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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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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR

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Nuclear Magnetic Resonance Study of Hydrogen-Bonded Ring Protons in Watson-Crick Base Pairs

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Measurement of15N-13C J couplings in staphylococcal nuclease

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Theoretical study of the effective Chemical Shielding Anisotropy (CSA) in peptide backbone, rating the impact of CSAs on the cross-correlated relaxations in L-alanyl-L-alanine

1 reference

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Chemical-shift anisotropy measurements of amide and carbonyl resonances in a microcrystalline protein with slow magic-angle spinning NMR spectroscopy

1 reference

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Limited variations in 15N CSA magnitudes and orientations in ubiquitin are revealed by joint analysis of longitudinal and transverse NMR relaxation

1 reference

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1 reference

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1 reference

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1 reference

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12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/20681720

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Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy

1 reference

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1 reference

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Identifiers

10.1021/JA103629E

1 reference

Europe PubMed Central

30 July 2017

release_2hpmsrcmnza75oeak4iqlzcpxi

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https://api.fatcat.wiki/v0/release/2hpmsrcmnza75oeak4iqlzcpxi

24 November 2022

based on heuristic

mapped directly with Wikidata item

1 reference

Europe PubMed Central

30 July 2017

1 reference

Europe PubMed Central

30 July 2017

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