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A Fractal Analysis of the Binding Kinetics of the Heat-Shock Protein Chaperone DnaK on a SPR Biosensor Surface

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A fractal analysis is presented for the binding kinetics of heat-shock protein chaperone DnaK in unstressed and stressed Escherichia coli cell lysate to anti-DnaK on a SPR biosensor chip surface or by ELISA. The binding kinetics is described by either a single-, dual-, or a triple-fractal analysis. As expected, the levels of chaperone DnaK expressed in stressed Escherichia coli cell lysate is higher than that expressed in unstressed Escherichia coli cell lysate. There is a change in the binding mechanism as one goes from a single- to a dual- to a triple-fractal analysis. The analysis provides values of the binding rate coefficient, k and the degree of heterogeneity on the sensing surface. Furthermore, the analysis provides fresh physical insights into the binding of Escherichia coli chaperone DnaK to anti-DnaK under unstressed and heat-stressed conditions.


Document Type: Research Article


Publication date: 2007-06-01

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