Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/95768
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Detecting selection for negative design in proteins through an improved model of the misfolded state |
Autor: | Minning, Jonas; Porto, Markus; Bastolla, Ugo CSIC ORCID | Palabras clave: | Negative design Protein folding Misfolding |
Fecha de publicación: | 2013 | Editor: | Wiley-Liss | Citación: | Proteins: Structure, Function and Genetics 81: 1102- 1112 (2013) | Resumen: | Proteins that need to be structured in their native state must be stable both against the unfolded ensemble and against incorrectly folded (misfolded) conformations with low free energy. Positive design targets the first type of stability by strengthening native interactions. The second type of stability is achieved by destabilizing interactions that occur frequently in the misfolded ensemble, a strategy called negative design. Here, we investigate negative design adopting a statistical mechanical model of the misfolded ensemble, which improves the usual Gaussian approximation by taking into account the third moment of the energy distribution and contact correlations. Applying this model, we detect and quantify selection for negative design in most natural proteins, and we analytically design protein sequences that are stable both against unfolding and against misfolding. © 2013 Wiley Periodicals, Inc. | URI: | http://hdl.handle.net/10261/95768 | DOI: | 10.1002/prot.24244 | Identificadores: | doi: 10.1002/prot.24244 issn: 0887-3585 |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
21
checked on 12-abr-2024
WEB OF SCIENCETM
Citations
19
checked on 23-feb-2024
Page view(s)
256
checked on 19-abr-2024
Download(s)
118
checked on 19-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.