(Q54537934)

English

A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides.

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scholarly article

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides. (English)

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

1

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

Wilfred F van Gunsteren

4

object named as

Wilfred F van Gunsteren

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

author name string

Christine Peter

2

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

Ruud M Scheek

3

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

Alan E Mark

5

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

publication date

1 July 2002

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

Journal of Biomolecular NMR

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

23

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

3

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

181-194

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

https://scigraph.springernature.com/pub.10.1023/a:1019854626147

0 references

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1 reference

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NMR cross-relaxation investigated by molecular dynamics simulation: a case study of ubiquitin in solution.

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The Protein Data Bank

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Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.

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Essential dynamics of proteins

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Convergence of sampling in protein simulations.

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Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

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Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations

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Assessing the effect of conformational averaging on the measured values of observables

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Raster3D Version 2.0. A program for photorealistic molecular graphics

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NMR structure of cysteinyl-phosphorylated enzyme IIB of the N,N'-diacetylchitobiose-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli

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Internal motional averaging and three-dimensional structure determination by nuclear magnetic resonance

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On the nature of molecular conformations inferred from high-resolution NMR.

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Calculation of NMR-relaxation parameters for flexible molecules from molecular dynamics simulations

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Identifiers

10.1023/A:1019854626147

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

Dimensions Publication ID

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12238590

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