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

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

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scholarly article

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Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

title

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

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Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

main subject

automation

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author name string

Roger Cole

series ordinal

1

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Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

J Patrick Loria

series ordinal

2

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stated in

Europe PubMed Central

PubMed publication ID

12766418

retrieved

26 June 2017

publication date

1 July 2003

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Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

published in

Journal of Biomolecular NMR

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Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

volume

26

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stated in

Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

issue

3

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stated in

Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

page(s)

203-213

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Europe PubMed Central

PubMed publication ID

12766418

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26 June 2017

cites work

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

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PubMed

reference URL

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

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12 December 2020

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Evidence for flexibility in the function of ribonuclease A

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PubMed

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

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12 December 2020

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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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PubMed

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

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12 December 2020

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

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PubMed

reference URL

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

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

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PubMed

reference URL

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

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12 December 2020

based on heuristic

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MOLMOL: a program for display and analysis of macromolecular structures

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PubMed

reference URL

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

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12 December 2020

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inferred from PubMed ID database lookup

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

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PubMed

reference URL

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

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12 December 2020

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

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PubMed

reference URL

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

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12 December 2020

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inferred from PubMed ID database lookup

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

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PubMed

reference URL

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

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12 December 2020

based on heuristic

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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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PubMed

reference URL

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

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12 December 2020

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inferred from PubMed ID database lookup

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

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PubMed

reference URL

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

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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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12 December 2020

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inferred from PubMed ID database lookup

The role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G.

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

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12 December 2020

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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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PubMed

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

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12 December 2020

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Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data

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12 December 2020

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Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales.

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12 December 2020

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

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PubMed

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

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based on heuristic

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

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PubMed

reference URL

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

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

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PubMed

reference URL

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

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Increased protein backbone conformational entropy upon hydrophobic ligand binding

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PubMed

reference URL

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

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1023/A:1023808801134

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stated in

Europe PubMed Central

PubMed publication ID

12766418

retrieved

26 June 2017

Dimensions Publication ID

1032775163

0 references

PubMed publication ID

12766418

1 reference

stated in

Europe PubMed Central

PubMed publication ID

12766418

retrieved

26 June 2017

 

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