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Thermodynamics biochemical

Thomas, P. G. Seelig, J., Binding of the calcium antagonist flunarizine to phosphatidylcholine bilayers Charge effects and thermodynamics, Biochem. J. 291, 3974-02 (1993). [Pg.272]

AG, is directly associated with the direction in which a particular chemical reaction can proceed. If AG < 0 for a given set of conditions of a particular reaction, then the reaction will proceed spontaneously in the indicated direction until equilibrium is reached. Conversely, if AG is positive, then energy will be needed to shift the reaction further from its equilibrium condition. See Helmholtz Energy Endergonic Exergonic Enthalpy Entropy Thermodynamics Biochemical Thermodynamics... [Pg.310]

Even the most complicated aspects of thermodynamics are based ultimately on three rather simple and straightforward laws. These laws and their extensions sometimes run counter to our intuition. However, once truly understood, the basic principles of thermodynamics become powerful devices for sorting out complicated chemical and biochemical problems. At this milestone in our scientific development, thermodynamic thinking becomes an enjoyable and satisfying activity. [Pg.57]

E. F. Vainstein Department of Kinetics and Thermodynamics of Cooperative Processes, N. M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia... [Pg.894]

Watanabe, T., and Nakamura, T. (1976). Studies on luciferase from Photobacterium phosphoreum. VIII. FMN-H2O2 initiated bioluminescence and the thermodynamics of the elementary steps of the luciferase reaction. J. Biochem. 79 489-495. [Pg.451]

The evolution of structures and mechanisms in plants to regulate water fluxes down these steep thermodynamic gradients and yet maintain the cellular conditions for biochemical activity was a major factor in the colonisation of the terrestrial habitat. Paradoxically, therefore, some water stress is completely normal , though some plants are better than others at accommodating large deviations. [Pg.102]

Ogston, AG SUpananta, P, The Thermodynamics of Interaction between Sephadex and Penetrating Solntes, Biochemical Jonmal 116, 171, 1970. [Pg.617]

The energy for the fission of the covalent bond in organic contaminants is normally supplied thermally using thermodynamically accessible chemical or biochemical reactions, or by the introduction of catalysts to lower the activation energy of the reactions. There has been interest, however, in using electrical energy in a number of forms to carry out these reactions. A selection of processes for the destruction of contaminant is noted with some illustrative examples. [Pg.37]

A. Miklavc, D. Kocjan, J. Mavri, J. Roller and D. Hadzi, On the fundamental difference in thermodynamics of agonist and antagonist interactions with P-adrenergic receptors and the mechanism of entropy-driven binding. Biochem. Pharmacol., 40 (1990) 663-669. [Pg.417]

Thermodynamics of adsorption at liquid interfaces has been well established [22-24]. Of particular interest in view of biochemical and pharmaceutical applications is the adsorption of ionic substances, as many of biologically active compounds are ionic under the physiological conditions. For studying the adsorption of ionic components at the liquid-liquid interface, the polarized liquid-liquid interface is advantageous in that the adsorption of ionic components can be examined by strictly controlling the electrical state of the interface, which is in contrast to the adsorption studies at the air-water or nonpolar oil-water interfaces [25]. [Pg.120]

H. M. Farrell, T. F. Kumosinski, P. Pulaski, and M. P. Thompson, Calcium-induced associations of the caeins a thermodynamic linkage approach to precipitation and resolubilization, Arch. Biochem. Bio-phys., 265, 146 (1988). [Pg.719]

Dalpiaz A, Townsend-Nicholson A, Beukers MW, Schofield P, Ijzerman AP. Thermodynamics of full agonist, partial agonist and antagonist binding to wild type and mutant adenosine Ai receptors. Biochem Pharmacol 1998 56 1437-1445. [Pg.249]

As we described in Chapter 3, the binding of reversible inhibitors to enzymes is an equilibrium process that can be defined in terms of the common thermodynamic parameters of dissociation constant and free energy of binding. As with any binding reaction, the dissociation constant can only be measured accurately after equilibrium has been established fully measurements made prior to the full establishment of equilibrium will not reflect the true affinity of the complex. In Appendix 1 we review the basic principles and equations of biochemical kinetics. For reversible binding equilibrium the amount of complex formed over time is given by the equation... [Pg.99]

There is a large amount of data available concerning the thermodynamic effects of ligands on other coordination sites (i. e., the thermodynamic cis- and iraws-effects). However, very little is known about the effects of ligands on the kinetic lability of other coordination sites. In fact, very little work has been carried out, directly with Bi2-derivatives, or with models of B12, on the kinetics of ligand substitution at the cobalt center. Of particular biochemical interest would be studies on the rate of displacement of coordinated benzimidazole by various ligands. Such work has not been reported at present. If the benzimidazole is replaced during enzymatic catalysis so that the lower axial position is occupied by some other Lewis base, one would expect this displacement, and the reverse step, to be very facile. This appears to be qualitatively true in that when water displaces benzimidazole as the benzimidazole is pro-... [Pg.91]

Oparin and his school in the Biochemical Institute in Moscow worked for many years with coacervate systems. For Oparin, the origin of life was the moment of formation of the first cell. Coacervates are today of only historical importance because of their low thermodynamic stability, they are considered dubious and too unstable. [Pg.266]

We emphasise that the next chapters refer only to the surface of Earth to which light and the atmosphere have access. This is a common restriction in the discussion of evolution but we shall have to examine also the geological and biochemical zones in (and beneath) the deep sea (in Chapter 11), where it appears that evolution could be taking a somewhat different and as yet less advanced route but based on the same principles. We emphasise that each chapter adds new uses of elements, of energy, of space, and of organisation with species variation as new chemotypes evolved. The thermodynamic characteristics of all cells are given in Table 4.11. [Pg.183]

Coming, P.A. (2002). Thermoeconomics beyond the second law. J. Bioeconom., 4, 57-88 Everett, D.H. (1959). An Introduction to Chemical Thermodynamics. Longmans, London Kinosita, K., Yasuda, R., Noji, H. and Adachi, K. (2000). A rotary molecular motor that can work at near 100% efficiency. Philos. Trans. Act. Royal Soc. London B, 355, 473—489. See also Proc. Biochem. Soc. (2005) Meeting Mechanics of Bioenergetic Membrane Proteins Structures and... [Pg.190]

R. Chambert and G. Gonzy-Treboul, Levansucrase of Bacillus subtilis Kinetic and thermodynamic aspects of transfructosylation processes, Eur. J. Biochem., 62 (1976) 55-64. [Pg.134]

D. Rentzeperis, L. A. Marky, T. J. Dwyer, B. H. Geirstanger, J. G. Pelton, and D. E. Wemmer, Interaction of minor groove ligands to an AAATT/AATTT site Correlation of thermodynamic characterization and solution structure, Biochem. 34 2937 (1995). [Pg.169]


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See also in sourсe #XX -- [ Pg.24 ]




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