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dc.contributor.authorFarhangi, Shiva
dc.contributor.authorDuhamel, Jean
dc.date.accessioned2017-09-25 19:37:53 (GMT)
dc.date.available2017-09-25 19:37:53 (GMT)
dc.date.issued2016-09-13
dc.identifier.urihttp://dx.doi.org/10.1021/acs.macromol.6b01295
dc.identifier.urihttp://hdl.handle.net/10012/12444
dc.descriptionThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Macromolecules, copyright © American Chemical Society after peer review and technical editing by publisher. To access the final edited and published work see http://dx.doi.org/10.1021/acs.macromol.6b01295en
dc.description.abstractOver the years, fluorescence quenching experiments have provided a robust analytical means to retrieve information about the internal dynamics of macromolecules in general and the long range polymer chain dynamics (LRPCD) of linear chains in particular. This report reviews the results obtained to. date with the two main fluorescence experiments based on collisional quenching that have been used over the years to describe LRPCD. These experiments involve the labeling of a chain with dyes and quenchers either at the ends of a monodisperse chain for fluorescence quenching end-to-end cyclization (fqEEC) experiments or randomly along a polydisperse chain for fluorescence decay analysis with the fluorescence blob model (FBM). The advantages and disadvantages of these two types Of experiments are discussed as well as their range of applications and applicability to the field of protein folding. In particular, this Perspective illustrates how fqEEc experiments are being applied to probe loop formation in polypeptides and how FBM analysis of randomly labeled polypeptides could help determine the size of foldons which are expected to solve Levinthal's long-standing paradox.en
dc.language.isoenen
dc.publisherAmerican Chemical Societyen
dc.subjectEnd-To-Enden
dc.subjectUnfolded Polypeptide-Chainsen
dc.subjectIntramolecular Contact Formationen
dc.subjectSingle-Molecule Freten
dc.subjectIntrinsically Disordered Proteinsen
dc.subjectPyrene Excimer Fluorescenceen
dc.subjectTriplet Energy-Transferen
dc.subjectCyclization Dynamicsen
dc.subjectSpectroscopic Ruleren
dc.subjectBlob Modelen
dc.titleLong Range Polymer Chain Dynamics Studied by Fluorescence Quenchingen
dc.typeArticleen
dcterms.bibliographicCitationFarhangi, S., & Duhamel, J. (2016). Long Range Polymer Chain Dynamics Studied by Fluorescence Quenching. Macromolecules, 49(17), 6149–6162. https://doi.org/10.1021/acs.macromol.6b01295en
uws.contributor.affiliation1Faculty of Scienceen
uws.contributor.affiliation2Chemistryen
uws.typeOfResourceTexten
uws.peerReviewStatusRevieweden
uws.scholarLevelFacultyen


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