This HTML5 document contains 45 embedded RDF statements represented using HTML+Microdata notation.

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

Namespace Prefixes

PrefixIRI
n11http://linked.opendata.cz/ontology/domain/vavai/riv/typAkce/
dctermshttp://purl.org/dc/terms/
n15http://localhost/temp/predkladatel/
n13http://purl.org/net/nknouf/ns/bibtex#
n16http://linked.opendata.cz/resource/domain/vavai/projekt/
n6http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n18http://linked.opendata.cz/ontology/domain/vavai/
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#
n8http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n19http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n7http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n17http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n5http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F00216224%3A14310%2F03%3A00009541%21RIV%2F2004%2FMSM%2F143104%2FN/
n20http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n14http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n9http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F03%3A00009541%21RIV%2F2004%2FMSM%2F143104%2FN
rdf:type
skos:Concept n18:Vysledek
dcterms:description
The inhibitory potency of four nanomolar diastereomeric inhibitors of HIV-1 protease [1] was studied by molecular dynamics simulations and MM-GBSA/PBSA analysis. As a starting point we used the crystal structures of protease-inhibitor complexes [2, 3]. Having added hydrogens, we surrounded the complexes with a box of explicit water molecules and added counterions to neutralize the box. Using AMBER 7 program package [4], we minimized, heated and equilibrated the system after which we ran 2-nanosecond-long production dynamics. Periodic boundary conditions were used and long-range electrostatics was treated by particle mesh Ewald (PME) technique. An analysis of the molecular dynamical trajectories was performed and their quality assessed. The protease-inhibitor binding energies were calculated with MM-GBSA/PBSA approach. The effect of the length of the simulation, method to calculate solvation energy, and other factors upon the results was determined. The inhibitory potency of four nanomolar diastereomeric inhibitors of HIV-1 protease [1] was studied by molecular dynamics simulations and MM-GBSA/PBSA analysis. As a starting point we used the crystal structures of protease-inhibitor complexes [2, 3]. Having added hydrogens, we surrounded the complexes with a box of explicit water molecules and added counterions to neutralize the box. Using AMBER 7 program package [4], we minimized, heated and equilibrated the system after which we ran 2-nanosecond-long production dynamics. Periodic boundary conditions were used and long-range electrostatics was treated by particle mesh Ewald (PME) technique. An analysis of the molecular dynamical trajectories was performed and their quality assessed. The protease-inhibitor binding energies were calculated with MM-GBSA/PBSA approach. The effect of the length of the simulation, method to calculate solvation energy, and other factors upon the results was determined.
dcterms:title
Nanosecond molecular dynamics of HIV protease-inhibitor complexes: Insight into the differential binding potency of diastereoisomers. Nanosecond molecular dynamics of HIV protease-inhibitor complexes: Insight into the differential binding potency of diastereoisomers. Nanosecond molecular dynamics of HIV protease-inhibitor complexes: Insight into the differential binding potency of diastereoisomers.
skos:prefLabel
Nanosecond molecular dynamics of HIV protease-inhibitor complexes: Insight into the differential binding potency of diastereoisomers. Nanosecond molecular dynamics of HIV protease-inhibitor complexes: Insight into the differential binding potency of diastereoisomers. Nanosecond molecular dynamics of HIV protease-inhibitor complexes: Insight into the differential binding potency of diastereoisomers.
skos:notation
RIV/00216224:14310/03:00009541!RIV/2004/MSM/143104/N
n3:strany
23-23
n3:aktivita
n17:P
n3:aktivity
P(LN00A016)
n3:dodaniDat
n9:2004
n3:domaciTvurceVysledku
n6:9309616
n3:druhVysledku
n14:D
n3:duvernostUdaju
n19:S
n3:entitaPredkladatele
n5:predkladatel
n3:idSjednocenehoVysledku
617152
n3:idVysledku
RIV/00216224:14310/03:00009541
n3:jazykVysledku
n7:cze
n3:klicovaSlova
HIV Protease, molecular dynamics
n3:klicoveSlovo
n8:molecular%20dynamics n8:HIV%20Protease
n3:kontrolniKodProRIV
[9C205A35AAE0]
n3:mistoKonaniAkce
Nové Hrady
n3:mistoVydani
Praha
n3:nazevZdroje
Materials in Structure Chemistry, Biology, Physics and Technology
n3:obor
n20:CF
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
3
n3:pocetUcastnikuAkce
0
n3:pocetZahranicnichUcastnikuAkce
0
n3:projekt
n16:LN00A016
n3:rokUplatneniVysledku
n9:2003
n3:tvurceVysledku
Kříž, Zdeněk Havlas, Zdeněk Lepšík, Martin
n3:typAkce
n11:CST
n3:zahajeniAkce
2003-01-01+01:00
s:issn
1211-5894
s:numberOfPages
1
n13:hasPublisher
Krystalografická společnost
n15:organizacniJednotka
14310