Binding process, description

While Eq. 7-12, known as the Adair equation,11 might seem to provide a complete description of the binding process, it usually does not. In many cases, there is more than one kind of binding site on a macromolecule and Eq. 7-12 tells us nothing about the distribution of the ligand X among different sites in complex PX. To consider this problem we must examine the microscopic binding constants. 

Evaluations of the interaction of P, with the hydrocarbonaceous ligates in terms of Eqs. (74)—(81), however, do not represent complete descriptions of the binding process, because the condition(s) under which the thermal energy of the system is increased has not been specified. If the heat capacity of the system is increased under experimental conditions where the pressure P does not change significantly, then Eq. (80) can be simplified and the specific heat capacity can be redefined as follows ... 

This chapter presents a brief summary of the essentials of statistics that are particularly appropriate for handling biochemical data. This is followed by a section on the quantitative analysis of experimental results which deals chiefly with binding processes and enzyme kinetics. The chapter concludes with a brief discussion of methods of sequence analysis and databases, including a description of the FASTA and Needleman and Wunsch algorithms which form the basis of most of the sequence alignment methods currently in use. 

In the Appendix to Chapter 7, we developed a quantitative description of the concerted model. Although developed to describe a binding process, the model also applies to enzyme activity because the fraction of enzyme active sites with substrate bound is proportional to enzyme activity. A key aspect of this model is the equilibrium between the T and the R states (p. 200), We defined L as the equilibrium constant between the R and the T forms. 

Electrostatic and van der Waals intermolecular interactions are involved in the binding process. Apart from a valid description of the conformational energies, accurate description of these interactions is crucial for the determination of intermolecular energies. The energy functions in the MM methods are normally parameterized against standard models, which involve interactions between atoms as in hydrogen... 

This chapter provides (i) a brief review of the chemistry involved in chiral host-chiral guest recognition involving primary amines (ii) a description of a nonchromatographic (equilibrium or bind-release based) separation process devel-... 

Real-time spectroscopic methods can be used to measure the binding, dissociation, and internalization of fluorescent ligands with cell-surface receptors on cells and membranes. The time resolution available in these methods is sufficient to permit a detailed analysis of complex processes involved in cell activation, particularly receptor-G protein dynamics. A description of the kinetics and thermodynamics of these processes will contribute to our understanding of the basis of stimulus potency and efficacy. 

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