Changes of protein stiffness during folding detect protein folding intermediates.

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dc.contributor.author Małek, Katarzyna E.
dc.contributor.author Szoszkiewicz, Robert
dc.date.accessioned 2014-05-09T13:21:01Z
dc.date.available 2014-05-09T13:21:01Z
dc.date.issued 2014-05-09
dc.identifier.uri http://hdl.handle.net/2097/17721
dc.description.abstract Single-molecule force-quench atomic force microscopy (FQ-AFM) is used to detect folding intermediates of a simple protein by detecting changes of molecular stiffness of the protein during its folding process. Those stiffness changes are obtained from shape and peaks of an autocorrelation of fluctuations in end-to-end length of the folding molecule. The results are supported by predictions of the equipartition theorem and agree with existing Langevin dynamics simulations of a simplified model of a protein folding. In the light of the Langevin simulations the experimental data probe an ensemble of random-coiled collapsed states of the protein, which are present both in the force-quench and thermal-quench folding pathways. en_US
dc.language.iso en_US en_US
dc.relation.uri http://link.springer.com/article/10.1007/s10867-013-9331-y en_US
dc.subject STM and AFM manipulations of a single molecule en_US
dc.subject Folding: thermodynamics, statistical mechanics, models, and pathways en_US
dc.subject Mechanical properties of molecules en_US
dc.title Changes of protein stiffness during folding detect protein folding intermediates. en_US
dc.type Article (author version) en_US
dc.date.published 2014 en_US
dc.citation.doi 10.1007/s10867-013-9331-y en_US
dc.citation.epage 23 en_US
dc.citation.issue 1 en_US
dc.citation.jtitle Journal of Biological Physics en_US
dc.citation.spage 15 en_US
dc.citation.volume 40 en_US
dc.contributor.authoreid szosz en_US


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