Biochemical processes biological energy

If we now suggest a correspondence between the formal model of FrBhlich and the dissipative subsytem(s) and the equilibrium system discussed in Section 3.1, one may consider the processes which are operative, including interactions with an external EM field, as depicted schematically in Fig. (7). No compelling experimental evidence exists that the equilibrium system made up of the ordinary aqueous dielectrics, Sections 2.3 to 2.7, shows the Bose-condensation which arises in the Frtfhlich theory. In fact, even systems of sufficient complexity to exhibit low-lying vibrational modes and structural subtlety to play a direct role in biochemical reactions at the interface between biochemical and biological processes [a-chymotrypsin (90-91), lysozyme (92 ) and DNA (93)], fail to show features not predicted by the methods of Section 2. Since collisional perturbations, even when non-reactive, will provide a source of the energy inputs, S, this implies the absence of non-linear terms (x=0,A=0), Eq. (14), for such systems. 

The ability to perform even the simplest of muscle movement requires complex coordination of the physical and chemical activities of the tissue. In recent years, nutritionists and exercise physiologists have described how the primary energy sources in food carbohydrates, fats, and proteins are transformed into the universal "currency" of biological energy, ATP. Oxidative metabolism processes the substrates through a cascade of enzymatic events to Insure maximal efficiency in energy conversion. At every level of this conversion, one or more metal ions serve as a cofactor to facilitate these biochemical reactions. The requirement of metals in the production of... 

AT any biochemical processes involve very rapid reactions and transient intermediates. Frequently the rapidity of the reaction causes major technical difficulties in ascertaining the details of the events occurring in the process. One approach to overcome this inherent problem is to utilize the fact that most chemical reactions are temperature dependent. This relationship is quantitatively described by the Arrhenius equation, k = Ae E /RT, where k represents the rate constant, A is a constant (the frequency factor), and Ea is the energy of activation. Consequently, by initiating the reaction at a sufficiently low temperature, interconversion of the intermediates may be effectively stopped and they may be accumulated and stabilized individually. Although the focus of this article is on the application of this low-temperature approach to the study of enzyme catalysis, that is, cryoenzymology, the technique is potentially of much wider biological application (1, 2,3). 

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