Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jmb.2005.05.070
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dc.titleThe folding mechanism of a dimeric β-barrel domain
dc.contributor.authorDe Prat-Gay, G.
dc.contributor.authorNadra, A.D.
dc.contributor.authorCorrales-Izquierdo, F.J.
dc.contributor.authorAlonso, L.G.
dc.contributor.authorFerreiro, D.U.
dc.contributor.authorMok, Y.-K.
dc.date.accessioned2014-10-27T08:42:28Z
dc.date.available2014-10-27T08:42:28Z
dc.date.issued2005-08-19
dc.identifier.citationDe Prat-Gay, G., Nadra, A.D., Corrales-Izquierdo, F.J., Alonso, L.G., Ferreiro, D.U., Mok, Y.-K. (2005-08-19). The folding mechanism of a dimeric β-barrel domain. Journal of Molecular Biology 351 (3) : 672-682. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jmb.2005.05.070
dc.identifier.issn00222836
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101914
dc.description.abstractThe dimeric β-barrel domain is an unusual topology, shared only by two viral origin binding proteins, where secondary, tertiary and quaternary structure are coupled, and where the dimerization interface is composed of two four-stranded half-β-barrels. The folding of the DNA binding domain of the E2 transcriptional regulator from human papillomavirus, strain-16, takes place through a stable and compact monomeric intermediate, with 31% the stability of the folded dimeric domain. Double jump multiple wavelength experiments allowed the reconstruction of the fluorescence spectrum of the monomeric intermediate at 100 milliseconds, indicating that tryptophan residues, otherwise buried in the folded state, are accessible to the solvent. Burial of surface area as well as differential behavior to ionic strength and pH with respect to the native ground state, plus the impossibility of having over 2500 Å2 of surface area of the half-barrel exposed to the solvent, indicates that the formation of a non-native compact tertiary structure precedes the assembly of native quaternary structure. The monomeric intermediate can dimerize, albeit with a weaker affinity (∼1 μM), to yield a non-native dimeric intermediate, which rearranges to the native dimer through a parallel folding channel, with a unimolecular rate-limiting step. Folding pathways from either acid or urea unfolded states are identical, making the folding model robust. Unfolding takes place through a major phase accounting for apparently all the secondary structure change, with identical rate constant to that of the fluorescence unfolding experiment. In contrast to the folding direction, no unfolding intermediate was found. © 2005 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jmb.2005.05.070
dc.sourceScopus
dc.subjectβ-barrel
dc.subjectDNA-binding
dc.subjectE2
dc.subjectFolding
dc.subjectPapillomavirus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.jmb.2005.05.070
dc.description.sourcetitleJournal of Molecular Biology
dc.description.volume351
dc.description.issue3
dc.description.page672-682
dc.description.codenJMOBA
dc.identifier.isiut000231099800018
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