By Arieh Y. Ben-Naim

This is often the 1st booklet that makes an attempt to review the starting place of cooperatvity in binding structures from the molecular standpoint. The molecular technique presents a deeper perception into the mechanism of cooperativity and rules, than the normal phenomenological process. This publication makes use of the instruments of statistical mechanics to provide the molecular concept of cooperativity. Cooperativity is utilized in a spread of processes-such as loading and unloading of oxygen at fairly small strain adjustments; holding a virtually consistent focus of varied compounds in dwelling cells; and switching on and rancid the interpreting of genetic details. This e-book can be utilized as a textbook by way of graduate scholars in Chemistry, Biochemistry and Biophysics, and also will be of curiosity to researchers in theoretical biochemistry.

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13) The thermodynamic stability requires that N be a monotonous increasing function of X. Due to the independence of the adsorbent molecules, the same is true also for n as a function of A,. The statistical mechanical interpretation of the stability condition is quite simple. From Eq. 14) This is the fluctuation, or the variance, of k for a single adsorbent molecule. 6). The latter is sometimes referred to as the binding capacity. It measures the amount of acid (or base) that should be added to the solution so that the pH will increase by one unit.

We assume that the internal degrees of freedom of both the adsorbent molecules and the ligands are unaffected by the binding process. No degrees of freedom are ascribed to the ligand occupying the binding site. When a ligand binds to the site, the energy change in the process is described by one parameter U9 referred to as the binding energy. , interchanging two ligands occupying different sites does not produce a new configuration. The ligands are supplied from an ideal gas reservoir; the only degree of freedom that changes upon binding is its translation.

Suppose the molecule has m binding sites, and the binding constant to the first site is k-^j) when the molecule is in state j. 5, we shall obtain a Langmuir isotherm with binding constant ^1 which is simply an average 2Jc1(J)Pj(Q), the sum being over all the states of the molecule. If there are m identical sites, the intrinsic binding constant is again ^1 = ^Lk1(J)P-(G). When a second ligand approaches the molecule, the conditional binding constant km might differ from ^1 for two conceptually different reasons.

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