Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/115893
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hospital Gasch, Adam | - |
dc.contributor.author | Candotti, Michela | - |
dc.contributor.author | Gelpí Buchaca, Josep Lluís | - |
dc.contributor.author | Orozco López, Modesto | - |
dc.date.accessioned | 2017-09-27T10:43:51Z | - |
dc.date.available | 2018-01-06T23:01:29Z | - |
dc.date.issued | 2017-01-06 | - |
dc.identifier.issn | 1520-6106 | - |
dc.identifier.uri | http://hdl.handle.net/2445/115893 | - |
dc.description.abstract | Extensive molecular dynamics (MD) simulations have been used to characterize the multiple roles of water in solvating different types of proteins under different environmental conditions. We analyzed a small set of proteins, representative of the most prevalent meta-folds under native conditions, in the presence of crowding agents, and at high temperature with or without high concentration of urea. We considered also a protein in the unfolded state as characterized by NMR and atomistic MD simulations. Our results outline the main characteristics of the hydration environment of proteins and illustrate the dramatic plasticity of water, and its chameleonic ability to stabilize proteins under a variety of conditions. | - |
dc.format.extent | 26 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Chemical Society | - |
dc.relation.isformatof | Versió postprint del document publicat a: https://doi.org/10.1021/acs.jpcb.6b09676 | - |
dc.relation.ispartof | Journal of Physical Chemistry B, 2017, vol. 121, num. 15, p. 3636-3643 | - |
dc.relation.uri | https://doi.org/10.1021/acs.jpcb.6b09676 | - |
dc.rights | (c) American Chemical Society, 2017 | - |
dc.source | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) | - |
dc.subject.classification | Dinàmica molecular | - |
dc.subject.classification | Urea | - |
dc.subject.classification | Altes temperatures | - |
dc.subject.classification | Proteïnes | - |
dc.subject.other | Molecular dynamics | - |
dc.subject.other | Urea | - |
dc.subject.other | High temperatures | - |
dc.subject.other | Proteins | - |
dc.title | The multiple roles of waters in protein solvation | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.identifier.idgrec | 666226 | - |
dc.date.updated | 2017-09-27T10:43:51Z | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/H2020/676559/EU//ELIXIR-EXCELERATE | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/H2020/675728/EU//BioExcel | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 28059510 | - |
Appears in Collections: | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona)) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
666226.pdf | 1.96 MB | Adobe PDF | View/Open |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.