Molecular dynamics studies of proteins
Identifieur interne : 000F81 ( Istex/Corpus ); précédent : 000F80; suivant : 000F82Molecular dynamics studies of proteins
Auteurs : Wilfred F. Van GunsterenSource :
- Current Opinion in Structural Biology [ 0959-440X ] ; 1993.
English descriptors
- KwdEn :
- Teeft :
- Aqueous solution, Basic conditions, Boundary conditions, Computer simulation, Crystal structure, Cytochrome p4socam, Dynamical properties, Dynamics, Electrostatic forces, Ensemble averages, Equilibrium properties, Experimental information, Force field, Free energy, Free energy calculation, Free energy change, Free energy differences, Inhibitor, Inhibitor binding, Initial configuration, Initial structure, Instantaneous restraints, Interatomic interaction function, Molecular, Molecular biophysics, Molecular dynamics, Molecular dynamics simulation, Molecular dynamics simulations, Molecular dynamics studies, Molecular dynamics study, Molecular system, Nato series, Phase space, Photosynthetic reaction center, Protein, Protein mutants, Protein structure, Relative stability, Sampling periods, Simulation, Simulation techniques, Spatial structure, Structural stability, Such simulations, Water molecules, White lysozyme.
Abstract
Molecular dynamics computer simulation studies of proteins are considered. Standard applications are the calculation of equilibrium properties, binding constants and the use of molecular dynamics simulation in the refinement of protein structure based on NMR or X-ray diffraction data. In addition, simulation of non-equilibrium processes and methodological studies are briefly discussed. Computer simulation is a very useful explorative tool with which to investigate protein structure, dynamics and function, provided it is used with a clear eye to its strengths and limitations.
Url:
DOI: 10.1016/S0959-440X(05)80164-2
Links to Exploration step
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<ce:abstract id="ab1" class="author" xml:lang="en"><ce:abstract-sec><ce:simple-para>Molecular dynamics computer simulation studies of proteins are considered. Standard applications are the calculation of equilibrium properties, binding constants and the use of molecular dynamics simulation in the refinement of protein structure based on NMR or X-ray diffraction data. In addition, simulation of non-equilibrium processes and methodological studies are briefly discussed. Computer simulation is a very useful explorative tool with which to investigate protein structure, dynamics and function, provided it is used with a clear eye to its strengths and limitations.</ce:simple-para>
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<ce:keywords class="abr" xml:lang="en"><ce:section-title>Abbreviations</ce:section-title>
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<tail><ce:bibliography><ce:section-title>References and recommended reading</ce:section-title>
<ce:bibliography-sec><ce:bib-reference id="bib1"><ce:label>1.</ce:label>
<sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>van Gunsteren</ce:surname>
<ce:given-name>WF</ce:given-name>
</sb:author>
<sb:author><ce:surname>Mark</ce:surname>
<ce:given-name>AE</ce:given-name>
</sb:author>
</sb:authors>
<sb:title><sb:maintitle>On the Interpretation of Bio-chemical Data by Molecular Dynamics Computer Simulation</sb:maintitle>
</sb:title>
</sb:contribution>
<sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Eur J Biochem</sb:maintitle>
</sb:title>
<sb:volume-nr>204</sb:volume-nr>
</sb:series>
<sb:date>1992</sb:date>
</sb:issue>
<sb:pages><sb:first-page>947</sb:first-page>
<sb:last-page>961</sb:last-page>
</sb:pages>
</sb:host>
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<ce:bib-reference id="bib2"><ce:label>••</ce:label>
<ce:note><ce:simple-para>Papers of particular interest, published within the annual period of review, have been highlighted as: of outstanding interest</ce:simple-para>
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