Cooperativity and Regulation in Biochemical Processes by Arieh Y. Ben-Naim

By Arieh Y. Ben-Naim

This can be the 1st publication that makes an attempt to review the starting place of cooperatvity in binding structures from the molecular perspective. The molecular method offers a deeper perception into the mechanism of cooperativity and legislation, than the normal phenomenological approach.
This e-book makes use of the instruments of statistical mechanics to give the molecular thought of cooperativity. Cooperativity is utilized in various processes-such as loading and unloading of oxygen at fairly small strain transformations; protecting a nearly consistent focus of assorted compounds in residing cells; and switching off and on the examining of genetic information.
This publication can be used as a textbook through graduate scholars in Chemistry, Biochemistry and Biophysics, and also will be of curiosity to researchers in theoretical biochemistry.

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Extra resources for Cooperativity and Regulation in Biochemical Processes

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At other times, it consists of the product of direct and indirect factors. Yet in other cases, the direct and indirect parts are so intertwined that no such factorization is possible. Examples of these cases will be discussed in Chapter 4. The polynomial within parentheses in Eq. 5) [or in the denominator of Eq. 6)] is called the binding polynomial and is used extensively in the phenomenological approach to binding systems. It is often identified (up to a multiplicative constant) with the partition function of the system.

6). 10) As an extreme example suppose we have two dipoles, as before. The equilibrium average interaction between them is always attractive [see Eq. 8)]. We now introduce a point charge of any sign as shown in Fig. 6. If the dipole-charge interaction is strong, it could orient the dipoles in such a way that the average dipole-dipole interaction will become repulsive. Clearly, similar effects will be observed when a third dipole is present. 1) becomes invalid. In spite of what we have seen above, we shall always assume the validity of Eq.

As such, they are phenomenological constants that do not reveal their dependence on the molecular properties of the system. On the other hand, the coefficients in the partition function are defined in terms of molecular parameters and therefore, in principle, are calculable from molecular properties of the binding system. Specifically, all possible sources of cooperativity may be studied from the coefficients of the partition function, but none can be extracted from the phenomenological binding constants.

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