This HTML5 document contains 53 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Namespace Prefixes

PrefixIRI
dctermshttp://purl.org/dc/terms/
n10http://localhost/temp/predkladatel/
n13http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n12http://linked.opendata.cz/resource/domain/vavai/projekt/
n17http://linked.opendata.cz/ontology/domain/vavai/
n9http://linked.opendata.cz/resource/domain/vavai/zamer/
n14http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F00216224%3A14310%2F04%3A00009962%21RIV08-MSM-14310___/
shttp://schema.org/
skoshttp://www.w3.org/2004/02/skos/core#
n3http://linked.opendata.cz/ontology/domain/vavai/riv/
n2http://linked.opendata.cz/resource/domain/vavai/vysledek/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n5http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n18http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n16http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n8http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n19http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n7http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n4http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F04%3A00009962%21RIV08-MSM-14310___
rdf:type
n17:Vysledek skos:Concept
dcterms:description
The interactions between the protein and the solvent were analyzed, and protein regions with a high density of water molecules, as well as structural water molecules, were determined by using molecular dynamics (MD) simulations. A number of water molecules that were in contact with the protein for the whole trajectory were determined. Their interaction energies and hydrogen bonds with protein residues were analyzed. Altogether, 39, 27, 49, and 32 water molecules bound to the protein were found for trajectories of the free CDK2, CDK2/ATP, CDK2/roscovitine, and CDK2/isopentenyladenine complexes, respectively. Positions of observed water molecules were compared with X-ray crystallography data. Special attention was paid to water molecules in the active site of the enzyme, and especially to the deep pocket, where the N9 roscovitine side-chain is buried. Exchange of active-site water molecules with bulk water through the tunnel from the pocket was observed. In the CDK2/isopentenyladenine complex simulation The interactions between the protein and the solvent were analyzed, and protein regions with a high density of water molecules, as well as structural water molecules, were determined by using molecular dynamics (MD) simulations. A number of water molecules that were in contact with the protein for the whole trajectory were determined. Their interaction energies and hydrogen bonds with protein residues were analyzed. Altogether, 39, 27, 49, and 32 water molecules bound to the protein were found for trajectories of the free CDK2, CDK2/ATP, CDK2/roscovitine, and CDK2/isopentenyladenine complexes, respectively. Positions of observed water molecules were compared with X-ray crystallography data. Special attention was paid to water molecules in the active site of the enzyme, and especially to the deep pocket, where the N9 roscovitine side-chain is buried. Exchange of active-site water molecules with bulk water through the tunnel from the pocket was observed. In the CDK2/isopentenyladenine complex simulation The interactions between the protein and the solvent were analyzed, and protein regions with a high density of water molecules, as well as structural water molecules, were determined by using molecular dynamics (MD) simulations. A number of water molecules that were in contact with the protein for the whole trajectory were determined. Their interaction energies and hydrogen bonds with protein residues were analyzed. Altogether, 39, 27, 49, and 32 water molecules bound to the protein were found for trajectories of the free CDK2, CDK2/ATP, CDK2/roscovitine, and CDK2/isopentenyladenine complexes, respectively. Positions of observed water molecules were compared with X-ray crystallography data. Special attention was paid to water molecules in the active site of the enzyme, and especially to the deep pocket, where the N9 roscovitine side-chain is buried. Exchange of active-site water molecules with bulk water through the tunnel from the pocket was observed. In the CDK2/isopentenyladenine complex simulation
dcterms:title
Analysis of CDK2 active-site hydration: A method to design new inhibitors Analýza hydratace CDK2 aktivního místa Analysis of CDK2 active-site hydration: A method to design new inhibitors
skos:prefLabel
Analysis of CDK2 active-site hydration: A method to design new inhibitors Analýza hydratace CDK2 aktivního místa Analysis of CDK2 active-site hydration: A method to design new inhibitors
skos:notation
RIV/00216224:14310/04:00009962!RIV08-MSM-14310___
n3:strany
258-274
n3:aktivita
n16:Z n16:P
n3:aktivity
P(GV201/98/K041), Z(MSM 143100005), Z(MSM 153100007)
n3:cisloPeriodika
3
n3:dodaniDat
n4:2008
n3:domaciTvurceVysledku
n13:5517680 n13:9309616 n13:4347374
n3:druhVysledku
n19:J
n3:duvernostUdaju
n18:S
n3:entitaPredkladatele
n14:predkladatel
n3:idSjednocenehoVysledku
554185
n3:idVysledku
RIV/00216224:14310/04:00009962
n3:jazykVysledku
n8:eng
n3:klicovaSlova
cyclin-dependent kinase; ATP; roscovitine; isopentenyladenine; molecular dynamics; hydration of proteins; structural water molecules
n3:klicoveSlovo
n5:cyclin-dependent%20kinase n5:molecular%20dynamics n5:roscovitine n5:structural%20water%20molecules n5:isopentenyladenine n5:ATP n5:hydration%20of%20proteins
n3:kodStatuVydavatele
CZ - Česká republika
n3:kontrolniKodProRIV
[54671841F086]
n3:nazevZdroje
Proteins: Structure, Function, and Bioinformatics
n3:obor
n7:CF
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n12:GV201%2F98%2FK041
n3:rokUplatneniVysledku
n4:2004
n3:svazekPeriodika
55
n3:tvurceVysledku
Kříž, Zdeněk Otyepka, Michal Koča, Jaroslav Bártová, Iveta
n3:zamer
n9:MSM%20143100005 n9:MSM%20153100007
s:issn
0887-3585
s:numberOfPages
17
n10:organizacniJednotka
14310