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Protein Folding

dc.contributor.authorCruzeiro, Leonor
dc.contributor.editorSpringborg, Michael
dc.date.accessioned2014-03-06T11:58:24Z
dc.date.available2014-03-06T11:58:24Z
dc.date.issued2010
dc.description.abstractThe existing experimental data on protein folding is briefly reviewed. It is argued that the optimal fit is within a multi-funnel shaped free energy landscape and a kinetic mechanism for folding. The possibility that the transient forces responsible for such a kinetic mechanism come from vibrational excited states (the VES hypothesis) is introduced. Two applications of the VES hypothesis to the structural instability of the proteins associated with misfolding diseases are presented. Finally, in the last section, a detailed kinetic mechanism is put forward according to which, in cells, the structure that polypeptide chains adopt, as they come out of the ribosome, is a helix, and the proposed general pathway followed by all amino acid sequences from this initial structure to the final three dimensional structure is described. An analysis is made of how the proposed kinetic mechanism can account for many of the experimentally observed features of protein folding. It is pointed out how this new kinetic mechanism, which was arrived at by the application of physical principles, may also help to derive a method of determining the tertiary structure of a protein from its primary sequence.por
dc.description.sponsorshipFundação para a Ciência e Tecnologiapor
dc.identifier.doihttp://dx.doi.org/10.1039/9781849730884-00089
dc.identifier.isbn978-1-84973-088-4
dc.identifier.otherAUT: LHA01632;
dc.identifier.urihttp://hdl.handle.net/10400.1/3578
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherRoyal Society of Chemistrypor
dc.relation.publisherversionhttp://www.rsc.org/shop/books/2010/9781847550750.asppor
dc.subjectProtein Foldingpor
dc.subjectVES hypothesispor
dc.titleProtein Foldingpor
dc.typebook part
dspace.entity.typePublication
oaire.citation.conferencePlaceU.K.por
oaire.citation.endPage114por
oaire.citation.startPage89por
oaire.citation.titleSPR - Chemical Modellingpor
oaire.citation.volume7por
rcaap.rightsrestrictedAccesspor
rcaap.typebookPartpor

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