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By Michael I Page
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Example text
The 0... 0 and the 0... 15 A,respectively. The force constant for 0... 0 stretching in ice is 121 kJ/mole/A and, if distortion from the equilibrium 0... 0 distance obeyed a quadratic expression such as Eqn. 48, the energy change as a function of distance would be as illustrated in Fig. 10. It is easier to stretch a hydrogen bond than it is to ENERGY kJ/rnole) / CCC ANGLE B// ,'H-BOND STRETCHING / NON-BONDED INTERACTIONS % CHANGE FROM OPTIMUM Fig. 10. The increase in energy brought about a change in the optimum parameter of a molecule as indicated.
We shall see later that such geometrical distortion does not, in any case, take place. Disulphide links Disulphide bridges are usually buried in the interior of proteins or deeply embedded in grooves. Recently, it has been suggested that these bonds provide elasticity and allow the enzyme to deform under stress. However, S-S bonds are strong covalent bonds which are not easily stretched or distorted. Although the stretching frequency of an S-S bond ( - 500/cm) is lower than that for C-C stretching ( - 1200/cm), the reduced mass is greater.
Estimation of binding energies Observed free energies of binding substrates to enzymes are often less than the intrinsic binding energy because much of the binding energy is “used up” in bringing about the required loss of entropy and in inducing any destabilisation of the substrate or enzyme. Observed enthalpy and entropy changes for binding or activation cannot be used to deduce binding energies because of the dominant role that the solvent water plays in determining the measured values. The intrinsic binding energy of a small group A may be obtained from a comparison of the free energies of binding the larger molecule B and the molecule A-B, where A is a covalently bound substituent.