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dc.contributor.authorLeite, VBP-
dc.contributor.authorOnuchic, J. N.-
dc.contributor.authorStell, G.-
dc.contributor.authorWang, J.-
dc.identifier.citationBiophysical Journal. Bethesda: Biophysical Society, v. 87, n. 6, p. 3633-3641, 2004.-
dc.description.abstractWe propose an approach to integrate the theory, simulations, and experiments in protein-folding kinetics. This is realized by measuring the mean and high-order moments of the first-passage time and its associated distribution. The full kinetics is revealed in the current theoretical framework through these measurements. In the experiments, information about the statistical properties of first-passage times can be obtained from the kinetic folding trajectories of single molecule experiments ( for example, fluorescence). Theoretical/simulation and experimental approaches can be directly related. We study in particular the temperature-varying kinetics to probe the underlying structure of the folding energy landscape. At high temperatures, exponential kinetics is observed; there are multiple parallel kinetic paths leading to the native state. At intermediate temperatures, nonexponential kinetics appears, revealing the nature of the distribution of local traps on the landscape and, as a result, discrete kinetic paths emerge. At very low temperatures, exponential kinetics is again observed; the dynamics on the underlying landscape is dominated by a single barrier. The ratio between first-passage-time moments is proposed to be a good variable to quantitatively probe these kinetic changes. The temperature-dependent kinetics is consistent with the strange kinetics found in folding dynamics experiments. The potential applications of the current results to single-molecule protein folding are discussed.en
dc.publisherBiophysical Society-
dc.sourceWeb of Science-
dc.titleProbing the kinetics of single molecule protein foldingen
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniv Calif San Diego-
dc.contributor.institutionSUNY Stony Brook-
dc.contributor.institutionChinese Acad Sci-
dc.description.affiliationUniv Estadual Paulista, Dept Fis, Inst Biociencias Letras & Ciências Exatas, Sao Jose do Rio Preto, Brazil-
dc.description.affiliationUniv Calif San Diego, Ctr Theoret Biol Phys, Dept Phys, La Jolla, CA 92093 USA-
dc.description.affiliationSUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA-
dc.description.affiliationChinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Electroanalyt Chem, Changchun 130022, Peoples R China-
dc.description.affiliationUnespUniv Estadual Paulista, Dept Fis, Inst Biociencias Letras & Ciências Exatas, Sao Jose do Rio Preto, Brazil-
dc.rights.accessRightsAcesso aberto-
dc.relation.ispartofBiophysical Journal-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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