About: Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations

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About: Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	High-pressure methods have become attractive tools for investigation of the structural stability of proteins. Besides protein unfolding, dimerization can be studied this way, too. HIV-1 protease is a convenient target of experimental and theoretical high-pressure studies. In this study molecular-dynamics simulations are used to predict the response of HIV-1 protease to the pressure of 0.1 to 600 MPa. The protease conformation of both the monomer and the dimer is highly rigid changing insignificantly with growing pressure. Hydrophobicity of the protease decreases with increasing pressure. Water density inside the active-site cavity grows from 87% to 100% of the bulk water density within the pressure range. The dimer-dissociation volume change is negative for most of the pressure ranges with the minimum of -105 ml mol-1, except for a short interval of positive values at low pressures. The dimer is thus slightly stabilized up to 160 MPa, but strongly destabilized by higher pressures. High-pressure methods have become attractive tools for investigation of the structural stability of proteins. Besides protein unfolding, dimerization can be studied this way, too. HIV-1 protease is a convenient target of experimental and theoretical high-pressure studies. In this study molecular-dynamics simulations are used to predict the response of HIV-1 protease to the pressure of 0.1 to 600 MPa. The protease conformation of both the monomer and the dimer is highly rigid changing insignificantly with growing pressure. Hydrophobicity of the protease decreases with increasing pressure. Water density inside the active-site cavity grows from 87% to 100% of the bulk water density within the pressure range. The dimer-dissociation volume change is negative for most of the pressure ranges with the minimum of -105 ml mol-1, except for a short interval of positive values at low pressures. The dimer is thus slightly stabilized up to 160 MPa, but strongly destabilized by higher pressures. (en)
Title	Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations (en)
skos:prefLabel	Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations (en)
skos:notation	RIV/70883521:28110/14:43871922!RIV15-MSM-28110___
http://linked.open...avai/riv/aktivita	V
http://linked.open...avai/riv/aktivity	V
http://linked.open...iv/cisloPeriodika	47
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Ingr, Marek Hrnčiřík, Josef Kutálková, Eva
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Tomáše Bati ve Zlíně / Fakulta technologická
http://linked.open...dnocenehoVysledku	39135
http://linked.open...ai/riv/idVysledku	RIV/70883521:28110/14:43871922
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	HIV-1 protease, high pressure, molecular dynamics, dimerization equilibrium, volume change (en)
http://linked.open.../riv/klicoveSlovo	volume change molecular dynamics high pressure HIV-1 protease dimerization equilibrium
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[7CE136EF67BA]
http://linked.open...i/riv/nazevZdroje	Physical Chemistry Chemical Physics
http://linked.open...in/vavai/riv/obor	CF
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	3 (xsd:int)
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	16
http://linked.open...iv/tvurceVysledku	Hrnčiřík, Josef Ingr, Marek Kutálková, Eva
issn	1463-9076
number of pages	10 (xsd:int)
http://bibframe.org/vocab/doi	10.1039/c4cp03676j
http://localhost/t...ganizacniJednotka	28110

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