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

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dc.title Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations en
dc.contributor.author Kutálková, Eva
dc.contributor.author Hrnčiřík, Josef
dc.contributor.author Ingr, Marek
dc.relation.ispartof Physical Chemistry Chemical Physics
dc.identifier.issn 1463-9076 Scopus Sources, Sherpa/RoMEO, JCR
dc.date.issued 2014
utb.relation.volume 16
utb.relation.issue 47
dc.citation.spage 25906
dc.citation.epage 25915
dc.type article
dc.language.iso en
dc.publisher Royal Society of Chemistry (RSC)
dc.identifier.doi 10.1039/c4cp03676j
dc.relation.uri http://pubs.rsc.org/en/Content/ArticleLanding/2014/CP/C4CP03676J#!divAbstract
dc.description.abstract 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
utb.faculty Faculty of Technology
dc.identifier.uri http://hdl.handle.net/10563/1003926
utb.identifier.obdid 43872177
utb.identifier.scopus 2-s2.0-84912042078
utb.identifier.wok 000345208200028
utb.identifier.coden PPCPF
utb.source j-scopus
dc.date.accessioned 2015-01-13T09:25:43Z
dc.date.available 2015-01-13T09:25:43Z
dc.description.sponsorship P41-RR005969, NIH, National Institutes of Health
dc.description.sponsorship National Institutes of Health [P41-RR005969]
dc.rights.access openAccess
utb.contributor.internalauthor Kutálková, Eva
utb.contributor.internalauthor Hrnčiřík, Josef
utb.contributor.internalauthor Ingr, Marek
utb.fulltext.affiliation Eva Kutálková, Josef Hrnčiřík and Marek Ingr* Tomas Bata University in Zlín, Faculty of Technology, Department of Physics and Materials Engineering, Nám. T.G. Masaryka 5555, 76001 Zlín, Czech Republic. E-mail: ingr@ft.utb.cz; Fax: +420 576035141; Tel: +420 576031417
utb.fulltext.dates Received 17th August 2014, Accepted 19th October 2014
utb.fulltext.sponsorship NAMD was developed by the Theoretical Biophysics Group in the Beckman Institute for Advanced Science and Technology at the University of Illinois at Urbana-Champaign (http://www.ks.uiuc. edu/Research/namd/). VMD has been developed by the Theoretical and Computational Biophysics Group at the Beckman Institute for Advanced Science and Technology of the University of Illinois at Urbana-Champaign. This work is supported by the National Institutes of Health under grant number P41-RR005969.
utb.fulltext.faculty Faculty of Technology
utb.fulltext.ou Department of Physics and Materials Engineering
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