English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/9416
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
DC FieldValueLanguage
dc.contributor.authorPeng, Li-
dc.contributor.authorOliva, Fabiana Y.-
dc.contributor.authorNaganathan, Athi N.-
dc.contributor.authorMuñoz, Víctor-
dc.date.accessioned2009-01-01T19:41:55Z-
dc.date.available2009-01-01T19:41:55Z-
dc.date.issued2008-12-31-
dc.identifier.citationProc. Natl. Acad. Sci. USA, DOI 10.1073/pnas.0802986106en_US
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10261/9416-
dc.descriptionSupporting information (12 pages) available at: http://www.pnas.org/content/suppl/2008/12/31/0802986106.DCSupplemental/0802986106SI.pdfen_US
dc.descriptionPublished online before print December 31, 2008.-
dc.description.abstractThe small helical protein BBL has been shown to fold and unfold in the absence of a free energy barrier according to a battery of quantitative criteria in equilibrium experiments, including probe-dependent equilibrium unfolding, complex coupling between denaturing agents, characteristic DSC thermogram, gradual melting of secondary structure, and heterogeneous atom-by-atom unfolding behaviors spanning the entire unfolding process. Here, we present the results of nanosecond T-jump experiments probing backbone structure by IR and end-to-end distance by FRET. The folding dynamics observed with these two probes are both exponential with common relaxation times but have large differences in amplitude following their probe-dependent equilibrium unfolding. The quantitative analysis of amplitude and relaxation time data for both probes shows that BBL folding dynamics are fully consistent with the one-state folding scenario and incompatible with alternative models involving one or several barrier crossing events. At 333 K, the relaxation time for BBL is 1.3 μs, in agreement with previous folding speed limit estimates. However, late folding events at room temperature are an order of magnitude slower (20 μs), indicating a relatively rough underlying energy landscape. Our results in BBL expose the dynamic features of one-state folding and chart the intrinsic time-scales for conformational motions along the folding process. Interestingly, the simple self-averaging folding dynamics of BBL are the exact dynamic properties required in molecular rheostats, thus supporting a biological role for one-state folding.en_US
dc.format.extent203 bytes-
dc.format.mimetypetext/plain-
dc.language.isoengen_US
dc.publisherNational Academy of Sciences (U.S.)en_US
dc.rightsclosedAccessen_US
dc.subjectDownhill foldingen_US
dc.subjectFolding landscapeen_US
dc.subjectLandscape topographyen_US
dc.subjectProtein dynamicsen_US
dc.subjectBiophysicsen_US
dc.titleDynamics of one-state downhill protein foldingen_US
dc.typeArtículoen_US
dc.identifier.doi10.1073/pnas.0802986106-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1073/pnas.0802986106en_US
Appears in Collections:(CIB) Artículos
Files in This Item:
There are no files associated with this item.
Show simple item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.