(Q30403423)

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Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin

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scholarly article

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Europe PubMed Central

21 June 2017

Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin (English)

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Europe PubMed Central

21 June 2017

molecular dynamics simulation

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protein structure determination

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Axel T. Brunger

2

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Europe PubMed Central

21 June 2017

3

object named as

Karplus M

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Europe PubMed Central

21 June 2017

author name string

Clore GM

1

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Europe PubMed Central

21 June 2017

Gronenborn AM

4

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Europe PubMed Central

21 June 2017

language of work or name

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publication date

1 October 1986

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Europe PubMed Central

21 June 2017

Journal of Molecular Biology

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Europe PubMed Central

21 June 2017

191

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Europe PubMed Central

21 June 2017

523-551

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Europe PubMed Central

21 June 2017

3

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Europe PubMed Central

21 June 2017

Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.

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Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

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An analysis of incorrectly folded protein models. Implications for structure predictions.

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Picosecond dynamics of tyrosine side chains in proteins

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Computer "Experiments" on Classical Fluids. I. Thermodynamical Properties of Lennard-Jones Molecules

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Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

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Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur

1 reference

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

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Secondary structure of the alpha-amylase polypeptide inhibitor tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance

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Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy

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Protein structural fluctuations during a period of 100 ps

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Dynamics of folded proteins

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Spatially constrained minimization of macromolecules

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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance

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1 reference

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A graphics model building and refinement system for macromolecules

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

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Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure

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An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution

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A protein structure from nuclear magnetic resonance data. lac repressor headpiece

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Restart procedures for the conjugate gradient method

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Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics.

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10.1016/0022-2836(86)90146-4

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Europe PubMed Central

21 June 2017

release_6jlptgzwm5g4zefydhgzs22fu4

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https://api.fatcat.wiki/v0/release/6jlptgzwm5g4zefydhgzs22fu4

24 November 2022

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Europe PubMed Central

21 June 2017

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