Protein Folding Dynamics of Cytochrome c Seen by Transient Grating and Transient Absorption Spectroscopies

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dc.contributor.authorChoi, Jungkweonko
dc.contributor.authorYang, Cheolheeko
dc.contributor.authorKim, Jeonghoko
dc.contributor.authorIhee, Hyotcherlko
dc.date.accessioned2019-03-07T12:13:41Z-
dc.date.available2019-03-07T12:13:41Z-
dc.date.created2012-02-06-
dc.date.issued2011-03-
dc.identifier.citationJOURNAL OF PHYSICAL CHEMISTRY B, v.115, no.12, pp.3127 - 3135-
dc.identifier.issn1520-6106-
dc.identifier.urihttp://hdl.handle.net/10203/250900-
dc.description.abstractWe investigate optically triggered protein folding dynamics of cytochrome c (Cytc) using transient grating (TG) and transient absorption (TA) spectroscopies. Despite many studies on protein folding dynamics of Cytc, a well-known model protein, direct spectroscopic evidence for the three-dimensional global folding process has been rarely reported. By measuring the TG signal of CO-bound Cytc (Cytc-CO) in the presence of a denaturant, we clearly detected the change of diffusion coefficient that reflects the size change of Cytc upon photodissociation of the CO ligand from unfolded Cytc-CO. The quantitative analysis of TG signals supports that the optically triggered folding reaction of Cytc in the presence of a denaturant takes place through a detectable intermediate (three-state folding kinetics). This is in contrast with the two-state folding dynamics of Cytc under a denaturant-free environment without any detectable intermediate.(1) From the quantitative global analysis of the TG signals, the rate constants for the U -> I and I -> N transitions in a CAPS buffer solution (pH 7) at room temperature in the presence of a denaturant at various concentrations are determined to be 1065 +/- 17 to 3476 +/- 103 s(-1) and 101 +/- 6 to 589 +/- 21 s(-1), respectively. In addition, the activation energies (E(a)) for the U -> I and I -> N transitions are determined to be 8.7 +/- 1.0 kcal/mol and 7.1 +/- 1.3 kcal/mol, respectively. The folding dynamics of Cytc initiated by the CO photolysis is discussed based in terms of the protein size change.-
dc.languageEnglish-
dc.publisherAMER CHEMICAL SOC-
dc.subjectRESOLVED CIRCULAR-DICHROISM-
dc.subjectX-RAY-SCATTERING-
dc.subjectFAST EVENTS-
dc.subjectINTERMOLECULAR INTERACTION-
dc.subjectDIFFUSION-COEFFICIENT-
dc.subjectELECTRON-TRANSFER-
dc.subjectCARBON-MONOXIDE-
dc.subjectKINETICS-
dc.subjectDENATURATION-
dc.subjectMOLECULES-
dc.titleProtein Folding Dynamics of Cytochrome c Seen by Transient Grating and Transient Absorption Spectroscopies-
dc.typeArticle-
dc.identifier.wosid000288644700050-
dc.identifier.scopusid2-s2.0-79953037296-
dc.type.rimsART-
dc.citation.volume115-
dc.citation.issue12-
dc.citation.beginningpage3127-
dc.citation.endingpage3135-
dc.citation.publicationnameJOURNAL OF PHYSICAL CHEMISTRY B-
dc.identifier.doi10.1021/jp106588d-
dc.contributor.localauthorIhee, Hyotcherl-
dc.contributor.nonIdAuthorChoi, Jungkweon-
dc.contributor.nonIdAuthorKim, Jeongho-
dc.type.journalArticleArticle-
dc.subject.keywordPlusRESOLVED CIRCULAR-DICHROISM-
dc.subject.keywordPlusX-RAY-SCATTERING-
dc.subject.keywordPlusFAST EVENTS-
dc.subject.keywordPlusINTERMOLECULAR INTERACTION-
dc.subject.keywordPlusDIFFUSION-COEFFICIENT-
dc.subject.keywordPlusELECTRON-TRANSFER-
dc.subject.keywordPlusCARBON-MONOXIDE-
dc.subject.keywordPlusKINETICS-
dc.subject.keywordPlusDENATURATION-
dc.subject.keywordPlusMOLECULES-
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