By Douglas A. Lauffenburger
Receptors: versions for Binding, Trafficking, and Signaling bridges the distance among chemical engineering and phone biology through lucidly and essentially demonstrating how a mathematical modeling procedure mixed with quantitative experiments promises superior realizing of phone phenomena regarding receptor/ligand interactions. In stressing the necessity for a quantitative realizing of the way receptor-mediated mobilephone capabilities rely on receptor and ligand homes, the publication bargains accomplished remedies of either simple and cutting-edge version frameworks that span the total spectrum of receptor processes--from basic phone floor binding, intracellular trafficking, and sign transduction occasions to the telephone behavioral services they govern, together with proliferation, adhesion, and migration. The e-book emphasizes mechanistic versions which are obtainable to experimental trying out and comprises precise examples of vital modern matters. This much-needed ebook introduces chemical engineers and bioengineers to big difficulties in receptor biology and familiarizes mobilephone biologists with the insights that may be won from engineering research and synthesis. As such, chemical engineers, researchers, and complex scholars within the fields of biotechnology, biomedical sciences, bioengineering, and molecular cellphone biology will locate this ebook to be conceptually wealthy, well timed, and valuable.
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Extra resources for By Douglas A. Lauffenburger - Receptors: Models for Binding, Trafficking, and Signaling: 1st (first) Edition
CELL SURFACE RECEPTOR/L1GAND BINDING FUNDAMENTALS 31 Figure 2-10 Graphical approaches to the determination of the association rate constant kf and the dissociation rate constant k, from experimental data, (a) The logarithm of the difference between the equilibrium and transient number of bound receptors, ln[Ceq — C(t)], is plotted versus time t. If KD and L0 are known, then k, can be determined from the slope. kt can then be determined from k T /K D . (b) koba, obtained from the slope of line plotted in (a), is graphed versus L0.
Expressed mathematically, these models allow kf = k fo (l + qfC) or kr = k ro (l + q,C) in Eqn. (2-8). The parameters qf and qr represent enhancement (when positive) or diminution (when negative) coefficients for association and dissociation rates, respectively. The work of DeLean and Rodbard identified underlying mathematical descriptions of the rate constants kf and kr with the form of experimental data that would be produced. First, if only kr varies with C, then Scatchard plots will be concave up or down for negative (qr > 0) and positive (qr < 0) cooperativity, respectively, but there can be no maxima or minima in these curves.
2-22). In such cases the simple model of Eqn. (2-1) is inadequate for accurate quantitative description of binding for use in models of receptor-mediated cell behavior. Curvature observed in Scatchard plots is typically termed cooperativity. Because the magnitude of the slope of the Scatchard curve is the effective receptor/ligand binding affinity (the reciprocal of the equilibrium dissociation constant, KD), cooperative binding refers to that in which KD - and, correspondingly, one or both of the rate constants, kf and kr - appear to vary with the extent of receptor occupancy by ligand (see Figure 2-11).