1. RODNA
  2. CONICET
  3. CONICET
Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.creatorKachlishvili, Khatuna-
dc.creatorMaisuradze, Gia G.-
dc.creatorMartín, Osvaldo Antonio-
dc.creatorLiwo, Adam-
dc.creatorVila, Jorge Alberto-
dc.creatorScheraga, Harold A.-
dc.date2017-12-21T20:33:16Z-
dc.date2017-12-21T20:33:16Z-
dc.date2014-06-
dc.date2017-12-12T18:38:22Z-
dc.date.accessioned2019-04-29T15:42:18Z-
dc.date.available2019-04-29T15:42:18Z-
dc.date.issued2014-06-
dc.identifierScheraga, Harold A.; Vila, Jorge Alberto; Liwo, Adam; Martín, Osvaldo Antonio; Maisuradze, Gia G.; Kachlishvili, Khatuna; et al.; Accounting for a mirror-image conformation as a subtle effect in protein folding; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 111; 23; 6-2014; 8458-8463-
dc.identifier0027-8424-
dc.identifierhttp://hdl.handle.net/11336/31297-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/299989-
dc.descriptionBy using local (free-energy profiles along the amino acid sequence and 13Cα chemical shifts) and global (principal component) analyses to examine the molecular dynamics of protein-folding trajectories, generated with the coarse-grained united-residue force field, for the B domain of staphylococcal protein A, we are able to (i) provide the main reason for formation of the mirror-image conformation of this protein, namely, a slow formation of the second loop and part of the third helix (Asp29?Asn35), caused by the presence of multiple local conformational states in this portion of the protein; (ii) show that formation of the mirror-image topology is a subtle effect resulting from local interactions; (iii) provide a mechanism for how protein A overcomes the barrier between the metastable mirror-image state and the native state; and (iv)<br />offer a plausible reason to explain why protein A does not remain in the metastable mirror-image state even though the mirror-image and native conformations are at least energetically compatible-
dc.descriptionFil: Kachlishvili, Khatuna. Cornell University; Estados Unidos-
dc.descriptionFil: Maisuradze, Gia G.. Cornell University; Estados Unidos-
dc.descriptionFil: Martín, Osvaldo Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis ; Argentina. Cornell University; Estados Unidos-
dc.descriptionFil: Liwo, Adam. University of Gdansk; Polonia-
dc.descriptionFil: Vila, Jorge Alberto. Cornell University; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Scheraga, Harold A.. Cornell University; Estados Unidos-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherNational Academy of Sciences-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/111/23/8458.abstract-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.1407837111-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectMISSFOLDING-
dc.subjectSYMETRICAL PROTEINS-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleAccounting for a mirror-image conformation as a subtle effect in protein folding-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: CONICET

Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro sencillo del ítem