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Transduction free energy

Calculation of Conformational Free Energies for a Model of a Bilobal Enzyme Protein kinases catalyze the transfer of phosphate from adenosine triphosphate (ATP) to protein substrates and are regulatory elements of most known pathways of signal transduction. [Pg.68]

Eisenberg, E. Hill, T.L. (1985). Muscle contraction and free energy transduction in biological systems. Science 227,999-1006. [Pg.235]

H. V. Westerhoff and K. van Dam, Thermodynamics and Control of Biological Free Energy Transduction, Elsevier, Amsterdam 1987. [Pg.249]

T. L. Hill, Free Energy Transduction in Biology, Academic Press, New York, 1977. [Pg.167]

Hill, T.L. Free Energy Transduction and Biochemical Cycle Kinetics, Springer-Verlag New York, 1989. [Pg.58]

Westerhoff, H.V. and Van Dam, K. (1987) Thermodynamics and Control of Biological Free-energy Transduction. (Amsterdam Elsevier Science Publishers B.V. (Biomedical Division)). [Pg.262]

Figure 13.12. Energy Transduction by Membrane Proteins. The Na+-K+ ATPase converts the free energy of phosphoryl transfer into the free energy of aNa+ ion gradient. The ion gradient can then be used to pump materials into the cell, through the action of a secondary transporter such as the Na+-glucose symporter. Figure 13.12. Energy Transduction by Membrane Proteins. The Na+-K+ ATPase converts the free energy of phosphoryl transfer into the free energy of aNa+ ion gradient. The ion gradient can then be used to pump materials into the cell, through the action of a secondary transporter such as the Na+-glucose symporter.

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See also in sourсe #XX -- [ Pg.360 ]




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