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• W3201991016 abstract "Publisher Summary The antifluorescein system provides a reasonable model to evaluate interfacial interactions utilizing transition-state theory. This system is advantageous for evaluating and quantitating interfacial chemistry. Binding of fluorescein ligand in the antifluorescein active site results in bathochromic shifts of the ligand's absorption spectrum and a decrease in both the fluorescence quantum yield and lifetime. These properties allow sensitive spectral and kinetic measurements to be made. Changes in the spectral and kinetic properties of a given antifluorescein antibody upon interacting with fluorescein attached to a carrier molecule compared to fluorescein thus provides important information about secondary force directed perturbations. Such forces, defined as those interactions exhibited outside of the classically defined antibody active site, have been demonstrated to modulate the conformation and free energy of binding of antifluorescein antibodies. The ability of the epitopic environment to influence antibody binding has obvious immunological ramifications. Dissection of those interactions that influence the overall dynamic and thermodynamics of a given protein system is of general importance in understanding interfacial protein chemistry. An understanding of interfacial protein chemistry requires evaluation of the thermodynamics of the system under investigation, as well as the energetic barriers responsible for the observed kinetics and affinity. Because of the kinetic methodology available for the antifluorescein system, the energetic barriers for complex decomposition can be evaluated. This chapter summarizes the results of a study, in which the energetic barriers of several protein/complex decompositions are analyzed utilizing transition-state theory. In essence, fluorescein 5-isothiocyanate is covalently linked to a variety of synthetic peptides and allows binding with the well defined high affinity 4-4-20 mAb. Differences in the rates of decomposition are measured at 275 K and 291 K and the height of energetic barriers calculated using classical transition-state analysis." @default.
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• W3201991016 title "Transition-state theory and secondary forces in antigen-antibody complexes" @default.
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