Downloads: 298

Files in This Item:
File Description SizeFormat 
nar_gku382.pdf1.31 MBAdobe PDFView/Open
Full metadata record
DC FieldValueLanguage
dc.contributor.authorHayashi, Tomohikoen
dc.contributor.authorOshima, Hirakuen
dc.contributor.authorMashima, Tsukasaen
dc.contributor.authorNagata, Takashien
dc.contributor.authorKatahira, Masatoen
dc.contributor.authorKinoshita, Masahiroen
dc.contributor.alternative木下, 正弘ja
dc.description.abstractIt is a central issue to elucidate the new type of molecular recognition accompanied by a global structural change of a molecule upon binding to its targets. Here we investigate the driving force for the binding of R12 (a ribonucleic acid aptamer) and P16 (a partial peptide of a prion protein) during which P16 exhibits the global structural change. We calculate changes in thermodynamic quantities upon the R12-P16 binding using a statistical-mechanical approach combined with molecular models for water which is currently best suited to studies on hydration of biomolecules. The binding is driven by a water-entropy gain originating primarily from an increase in the total volume available to the translational displacement of water molecules in the system. The energy decrease due to the gain of R12-P16 attractive (van der Waals and electrostatic) interactions is almost canceled out by the energy increase related to the loss of R12-water and P16-water attractive interactions. We can explain the general experimental result that stacking of flat moieties, hydrogen bonding and molecular-shape and electrostatic complementarities are frequently observed in the complexes. It is argued that the water-entropy gain is largely influenced by the geometric characteristics (overall shapes, sizes and detailed polyatomic structures) of the biomolecules.en
dc.publisherOxford University Pressen
dc.rights© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.en
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.titleBinding of an RNA aptamer and a partial peptide of a prion protein: crucial importance of water entropy in molecular recognition.en
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.jtitleNucleic acids researchen
dcterms.accessRightsopen access-
Appears in Collections:Journal Articles

Show simple item record

Export to RefWorks

Export Format: 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.