Detailing Protein Landscapes under Pressure

dc.creatorEspada, Rocío
dc.creatorSánchez Miguel, Ignacio Enrique
dc.creatorFerreiro, Diego
dc.date.accessioned2018-08-14T18:52:57Z
dc.date.accessioned2018-11-06T15:24:29Z
dc.date.available2018-08-14T18:52:57Z
dc.date.available2018-11-06T15:24:29Z
dc.date.created2018-08-14T18:52:57Z
dc.date.issued2016-12
dc.identifierEspada, Rocío; Sánchez Miguel, Ignacio Enrique; Ferreiro, Diego; Detailing Protein Landscapes under Pressure; Cell Press; Biophysical Journal; 111; 11; 12-2016; 2339-2341
dc.identifier0006-3495
dc.identifierhttp://hdl.handle.net/11336/55458
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1896826
dc.description.abstractNatural protein molecules are remarkablephysical objects. Despite the astronomicalnumber of competing structuralforms, these systems self-organize intobeautiful structural ensembles in biologicallyshort timescales, puzzlingout the feat of specifically bringingtogether thousands of atoms interactingby a myriad of weak forces. Moreover,most protein domains appear to foldwith ease in a deceptively simple twostatemanner, populating either the fullyfolded or fully unfolded ensembles.This is certainly not a property ofrandom amino acid chains.how doproteins do it?
dc.languageeng
dc.publisherCell Press
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.bpj.2016.10.038
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349516309973
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectProtein Folding
dc.subjectFolding Landscape
dc.subjectRepeat protein
dc.titleDetailing Protein Landscapes under Pressure
dc.typeArtículos de revistas
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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