Molecular Dynamics Study of Protein-Ligand Interactions

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00013838" target="_blank" >RIV/00216224:14310/05:00013838 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Molecular Dynamics Study of Protein-Ligand Interactions

Original language description

Detailed knowledge of interactions inside the proteins plays an important role in drug design. Experimental methods such as X-crystallography, NMR spectroscopy and neutron diffraction are typical experimental methods to analyze these interactions at atomic level. These experimental methods can, in some cases, be complemented by molecular modeling methods. The molecular docking combined with flexible conformational search, molecular dynamics and quantum dynamics are the most used modeling methods at thistime. Recently, the interactions of solvent molecules with cyclin dependent kinase (CDK2) using molecular dynamics were studied in our laboratory [1]. The previous study was extended by including solvation into interaction energies between protein and ligands acording to ref. [2]. Our molecular dynamics study was performed on complexes of cyclin-dependent kinase CDK2 with natural substrate ATP and with inhibitors roscovitine, olomoucine [3] and olomoucine II [4]. The X-ray crystallograp

Czech name

Studioum interakci protein-ligand pomoci molekulove dynamiky

Czech description

Detailed knowledge of interactions inside the proteins plays an important role in drug design. Experimental methods such as X-crystallography, NMR spectroscopy and neutron diffraction are typical experimental methods to analyze these interactions at atomic level. These experimental methods can, in some cases, be complemented by molecular modeling methods. The molecular docking combined with flexible conformational search, molecular dynamics and quantum dynamics are the most used modeling methods at thistime. Recently, the interactions of solvent molecules with cyclin dependent kinase (CDK2) using molecular dynamics were studied in our laboratory [1]. The previous study was extended by including solvation into interaction energies between protein and ligands acording to ref. [2]. Our molecular dynamics study was performed on complexes of cyclin-dependent kinase CDK2 with natural substrate ATP and with inhibitors roscovitine, olomoucine [3] and olomoucine II [4]. The X-ray crystallograp

Type

D - Article in proceedings

CEP classification

CF - Physical chemistry and theoretical chemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2005

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection

Cellular and Molecular Biology Letters

ISBN

1425-8153

ISSN

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e-ISSN

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Number of pages

2

Pages from-to

111-112

Publisher name

Department of Genetic Biochemistry, Institute of Biochemistry, University of Wroclaw

Place of publication

Wroclaw

Event location

Warsaw

Event date

Jun 25, 2005

Type of event by nationality

WRD - Celosvětová akce

UT code for WoS article

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