(Q36437269)

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Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding

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Europe PubMed Central

PubMed publication ID

14 August 2017

Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding (English)

1 reference

Europe PubMed Central

PubMed publication ID

14 August 2017

protein folding

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protein structure

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ORCID Public Data File 2021

author name string

Nilges M

1

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Europe PubMed Central

PubMed publication ID

14 August 2017

Clore GM

2

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14 August 2017

Gronenborn AM

3

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14 August 2017

language of work or name

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publication date

1 October 1988

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14 August 2017

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Europe PubMed Central

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14 August 2017

239

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14 August 2017

1

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Europe PubMed Central

PubMed publication ID

14 August 2017

129-136

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Europe PubMed Central

PubMed publication ID

14 August 2017

Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm

1 reference

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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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Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin

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

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NMR-pseudoenergy approach to the solution structure of acyl carrier protein

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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

1 reference

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Determination of three-dimensional protein structures from nuclear magnetic resonance data using fragments of known structures

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Calculation of protein conformation by the build-up procedure. Application to bovine pancreatic trypsin inhibitor using limited simulated nuclear magnetic resonance data

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Variable-target-function and build-up procedures for the calculation of protein conformation. Application to bovine pancreatic trypsin inhibitor using limited simulated nuclear magnetic resonance data

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Method of modeling protein structure by the two-dimensional nuclear magnetic resonance spectroscopy data; application to the proteinase inhibitor BUSI IIA from bull seminal plasma

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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations

1 reference

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21 January 2018

Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2.

1 reference

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Optimization by Simulated Annealing

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Crystallographic R factor refinement by molecular dynamics

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

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Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution

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Equation of State Calculations by Fast Computing Machines

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

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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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Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data

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Solution structures of the rabbit neutrophil defensin NP-5.

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Restart procedures for the conjugate gradient method

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A comparison of the restrained molecular dynamics and distance geometry methods for determining three-dimensional structures of proteins on the basis of interproton distances

1 reference

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Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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21 January 2018

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10.1016/0014-5793(88)80559-3

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Europe PubMed Central

PubMed publication ID

14 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

14 August 2017

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