FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data (Q30797308)

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Language	Label	Description	Also known as
English	FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

26 June 2017

FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data (English)

1 reference

Europe PubMed Central

PubMed publication ID

26 June 2017

0 references

author name string

Roger Cole

1

1 reference

Europe PubMed Central

PubMed publication ID

26 June 2017

J Patrick Loria

2

1 reference

Europe PubMed Central

PubMed publication ID

26 June 2017

publication date

1 July 2003

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Europe PubMed Central

PubMed publication ID

26 June 2017

Journal of Biomolecular NMR

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Europe PubMed Central

PubMed publication ID

26 June 2017

26

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Europe PubMed Central

PubMed publication ID

26 June 2017

3

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Europe PubMed Central

PubMed publication ID

26 June 2017

203-213

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Europe PubMed Central

PubMed publication ID

26 June 2017

15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding

1 reference

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Evidence for flexibility in the function of ribonuclease A

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Backbone dynamics of ribonuclease T1 and its complex with 2'GMP studied by two-dimensional heteronuclear NMR spectroscopy

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The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)

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An improved method for distinguishing between anisotropic tumbling and chemical exchange in analysis of 15N relaxation parameters

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MOLMOL: a program for display and analysis of macromolecular structures

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15N backbone dynamics of the S-peptide from ribonuclease A in its free and S-protein bound forms: toward a site-specific analysis of entropy changes upon folding

1 reference

https://pubmed.ncbi.nlm.nih.gov/12766418

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Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding

1 reference

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Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation

1 reference

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Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.

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Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA

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Evidence for a Functional Role of the Dynamics of Glycine-121 ofEscherichia coliDihydrofolate Reductase Obtained from Kinetic Analysis of a Site-Directed Mutant

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Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1.

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Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data

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NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding

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Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields

1 reference

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Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme

1 reference

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Increased protein backbone conformational entropy upon hydrophobic ligand binding

1 reference

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Identifiers

10.1023/A:1023808801134

1 reference

Europe PubMed Central

PubMed publication ID

26 June 2017

Dimensions Publication ID

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

26 June 2017

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