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Consilient protein-based energy conversions

T, to a new value of T, caused by an energy input represented by % to provide a measure of the change in Gibbs free energy for hydrophobic association of the protein-based polymer. Therefore, Tt, the onset temperature for the inverse temperature transition, represents an intrinsic property of the hydrophobic consilient mechanism of energy conversion. [Pg.131]

Systematic Classification of Energy Conversions by Consilient Protein-based Machines... [Pg.168]

More to the point, we now see biology s access to energy by means of the consilient mechanism of energy conversion, combined with readily available mutations to improve protein-based machines, as the source of increased structural order and functional diversity. [Pg.229]

In general, then, the energy conversions of biology reduce to the production of ATP and the uses of ATP, that is, the production of ATP by the five protein-based machines of the inner mitochondrial membrane and the thousands of subsequent protein-based machines that do the necessary work of the cell. This constitutes yet an enormous task that will fill hundreds of volumes in the future of protein-based machines. The intention of this volume, however, is to add a simplifying feature of a common groundwork of explanation for each of the hydrophobic and elastic consilient mechanisms. For the function of protein-based machines of biology, this perspective recovers an attractive element of simplification. [Pg.355]

Chapter 5 presents in one place, more extensively and in a more advanced state than previously, the decades long development of the comprehensive hydrophobic effect, the underpinnings of the hydrophobic consilient mechanism, whereby the control of hydrophobic association commands diverse energy conversion functions of protein-based polymers. Chapters 7 and 8 demonstrate the comprehensive hydrophobic effect and its interlinked elastic consilient mechanism to be vital aspects of protein function and dysfunction in biology. In the present chapter, we utilize this developed capacity to engineer protein-based polymers to demonstrate a few of an extraordinary range of applications. [Pg.456]

The above three discussed protein-based machines—Complex III of the electron transport chain, ATP synthase/Fj-ATPase, and the myosin II motor of muscle contraction—represent the three major classes of energy conversion that sustain Life. Therefore, the facility with which the consilient mechanisms explain their function indeed support the thesis that biology s vital force arises from the coupled hydrophobic and elastic consilient mechanisms. [Pg.561]

When taken together, the successes of the hydrophobic and consilient mechanisms in describing the functions of these three representative classes of biological energy conversion constitute a significant statement in favor of the roles of these mechanisms as vital forces that impart junction to the protein-based machines of biology. [Pg.561]


See other pages where Consilient protein-based energy conversions is mentioned: [Pg.125]    [Pg.107]    [Pg.154]    [Pg.236]    [Pg.642]    [Pg.36]    [Pg.102]    [Pg.103]    [Pg.104]    [Pg.124]    [Pg.128]    [Pg.132]    [Pg.136]    [Pg.168]    [Pg.170]    [Pg.176]    [Pg.204]    [Pg.210]    [Pg.218]    [Pg.224]    [Pg.235]    [Pg.332]    [Pg.332]    [Pg.382]    [Pg.449]    [Pg.460]    [Pg.461]    [Pg.546]    [Pg.549]    [Pg.567]    [Pg.641]    [Pg.643]   
See also in sourсe #XX -- [ Pg.168 , Pg.169 , Pg.170 , Pg.171 , Pg.172 , Pg.173 , Pg.174 , Pg.175 ]




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