(Q52082395)

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Correlation between changes in nuclear magnetic resonance order parameters and conformational entropy: molecular dynamics simulations of native and denatured staphylococcal nuclease.

scientific article published in February 2000

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

Correlation between changes in nuclear magnetic resonance order parameters and conformational entropy: molecular dynamics simulations of native and denatured staphylococcal nuclease. (English)

1 reference

Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

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Wrabl JO

1

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

Shortle D

2

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

Woolf TB

3

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

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publication date

1 February 2000

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

1 reference

Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

38

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

2

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Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

123-133

1 reference

Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

Insights into the local residual entropy of proteins provided by NMR relaxation

1 reference

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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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Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation.

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Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study

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21 January 2018

Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

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Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

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The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 A

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The crystal structure of staphylococcal nuclease refined at 1.7 A resolution

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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All-atom empirical potential for molecular modeling and dynamics studies of proteins

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Canonical dynamics: Equilibrium phase-space distributions

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The contribution of vibrational entropy to molecular association. The dimerization of insulin.

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Configurational entropy of native proteins

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Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamic models.

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Comparison of MD Simulations and NMR Experiments for Hen Lysozyme. Analysis of Local Fluctuations, Cooperative Motions, and Global Changes

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Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin

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Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease

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On the decomposition of free energies

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Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures

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A unified formulation of the constant temperature molecular dynamics methods

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Multidimensional free-energy calculations using the weighted histogram analysis method

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21 January 2018

Identifiers

10.1002/(SICI)1097-0134(20000201)38:2<123::AID-PROT2>3.0.CO;2-H

1 reference

Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 April 2018

http://europepmc.org/abstract/MED/10656260

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