Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/8022
COMPARTIR / EXPORTAR:
SHARE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Leo-Macías, Alejandra | - |
dc.contributor.author | López-Romero, Pedro | - |
dc.contributor.author | Lupyan, Dmitry | - |
dc.contributor.author | Zerbino, Daniel | - |
dc.contributor.author | Ortiz, Ángel R. | - |
dc.date.accessioned | 2008-10-27T15:29:21Z | - |
dc.date.available | 2008-10-27T15:29:21Z | - |
dc.date.issued | 2004-11-12 | - |
dc.identifier.citation | Biophysical Journal 88:1291-1299 (2005) | en_US |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.uri | http://hdl.handle.net/10261/8022 | - |
dc.description.abstract | An analysis is presented on how structural cores modify their shape across homologous proteins, and whether or not a relationship exists between these structural changes and the vibrational normal modes that proteins experience as a result of the topological constraints imposed by the fold. A set of 35 representative, well-populated protein families is studied. The evolutionary directions of deformation are obtained by using multiple structural alignments to superimpose the structures and extract a conserved core, together with principal components analysis to extract the main deformation modes from the three-dimensional superimposition. In parallel, a low-resolution normal mode analysis technique is employed to study the properties of the mechanical core plasticity of these same families. We show that the evolutionary deformations span a low dimensional space of 4–5 dimensions on average. A statistically significant correspondence exists between these principal deformations and the 20 slowest vibrational modes accessible to a particular topology. We conclude that, to a significant extent, the structural response of a protein topology to sequence changes takes place by means of collective deformations along combinations of a small number of low-frequency modes. The findings have implications in structure prediction by homology modeling. | en_US |
dc.description.sponsorship | This work was funded by grant BIO2001–3745 from the Spanish MCYT. A.L.M. is an FPI predoctoral fellow. D.L. is a predoctoral fellow of the PhD program of the Mount Sinai School of Medicine, New York. D.Z. is the recipient of a visiting fellowship from the Ecole Polytechnique (France). Research at Centro de Biología Molecular "Severo Ochoa" is facilitated by an institutional grant from Fundación Ramón Areces. | en_US |
dc.format.extent | 273275 bytes | - |
dc.format.extent | 333556 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | Biophysical Society | en_US |
dc.rights | openAccess | en_US |
dc.subject | Protein superfamilies | en_US |
dc.title | An Analysis of Core Deformations in Protein Superfamilies | en_US |
dc.type | artículo | en_US |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://www.biophysj.org/cgi/content/abstract/biophysj.104.052449v1 | en_US |
dc.identifier.e-issn | 1542-0086 | - |
dc.contributor.funder | Ministerio de Ciencia y Tecnología (España) | - |
dc.contributor.funder | Icahn School of Medicine at Mount Sinai | - |
dc.contributor.funder | École Polytechnique (France) | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100006280 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100007277 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.openairetype | artículo | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
ALeo-Macias_BiophysJ_1291.pdf | Main text | 266,87 kB | Adobe PDF | Visualizar/Abrir |
ALeo-Macias_BiochemJ_Suppl.pdf | 325,74 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
Page view(s)
367
checked on 23-abr-2024
Download(s)
342
checked on 23-abr-2024
Google ScholarTM
Check
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.