Conformational change of proteins arising from normal mode calculations (Q42646780)

4 November 2017

Conformational change of proteins arising from normal mode calculations (English)

1 reference

4 November 2017

Tama F

1

1 reference

PubMed ID

11287673

4 November 2017

Sanejouand YH

series ordinal

2

1 reference

4 November 2017

1 January 2001

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Protein Engineering Design and Selection

4 November 2017

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4 November 2017

14

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4 November 2017

1

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4 November 2017

1-6

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Essential dynamics of proteins

4 November 2017

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

A mutant T4 lysozyme displays five different crystal conformations

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

A database of macromolecular motions

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Normal mode analysis of human lysozyme: study of the relative motion of the two domains and characterization of the harmonic motion

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Collective variable description of native protein dynamics.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Analysis of domain motions by approximate normal mode calculations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Conformational change in the activation of lipase: an analysis in terms of low-frequency normal modes

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Molecular dynamics of an alpha-helical polypeptide: Temperature dependence and deviation from harmonic behavior

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Hinge-bending motion in citrate synthase arising from normal mode calculations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Computation of low-frequency normal modes in macromolecules: improvements to the method of diagonalization in a mixed basis and application to hemoglobin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Time dependence of atomic fluctuations in proteins: analysis of local and collective motions in bovine pancreatic trypsin inhibitor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

Citrate synthase: structure, control, and mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.1.1

21 January 2018

Identifiers

DOI

10.1093/PROTEIN/14.1.1

1 reference

4 November 2017

1 reference

PubMed ID

11287673