Efficiency consilient mechanism

We again draw comparison by quoting from Schrddinger s What is Life as published in 1944 What I wish to make clear in this last chapter is, in short, that from all that we have learnt about the structure of living matter, we must be prepared to find it working in a manner that cannot be reduced to the ordinary laws of physics. In the present volume, our foundation is, of course, the somewhat counterintuitive inverse temperature transition. It is by means of the inverse temperature transition that the energies essential to sustain Life can, in fact, be accessed. This efficient consilient mechanism, however, requires no new laws of physics. In fact, the seeds of this mechanism are found in a 1937 report of Butler,in which he analyzed the thermodynamic elements of the solubility of oil-like groups in water. 

Consilient Mechanisms for Diverse Protein-based Machines The Efficient Comprehensive Hydrophobic Effect... 

Importance of the Elastic Consilient Mechanism to Efficiency of Energy Conversion... 

AG ha Provides an Efficiency Limit and Becomes the Coupling Process in Energy Conversion by the Consilient Mechanism... 

Consilient Mechanism s Efficiency Limit, 6cm, for Model Protein Composition and Energy Source... 

The efficiency limit of the consilient mechanism for a chemical energy input is written as... 

Relative Chemomechanical Transductional Efficiencies of the Electrostatic Charge-Charge Repulsion and Consilient Mechanisms by Experimental Determination of Ap, An, and fAL... 

As shown in the inset of Figure 5.34, the Hill coefficient for PMA is 0.5, whereas that of Model Protein v is 2.7. Thus, without consideration of differences in An, the relative efficiency would be 0.5/8.0 = 0.06 or one-sixteenth as efficient as the model protein. After the statement of efficiency for chemomechanical transduction immediately below, the relative efficiency of the two mechanisms will be given using Model Protein iv as the representative of the consilient mechanism. The ratio of Hill coefficients for the latter model protein is 0.5/2.7 or differing only by a factor of 5 rather than 16. The experimentally determined relative efficiency is still very large. 

Thus the fundamental predictions of the hydrophobic elastic consilient mechanism are that the rotor would exhibit asymmetric hydrophobicity, that different arrangements of nucleotide analogues representing different states of polarity at the catalytic sites would orient the rotor, and that hydrolysis of ATP in formation of the most polar state at a catalytic site of the involved protein subunit(s) would demonstrate a near-ideal elastic deformation of the y-rotor and the protein subunit(s). Of course, such a mechanism would exhibit high efficiency and reversibility. 

By the hydrophobic consilient mechanism, the a-ATP sites provide a critical role of establishing a triangulation of repulsive forces that serves to limit the hydrophobic associations of the y-rotor. This triangulation of repulsive forces prevents the occurrence of a frictional drag on rotor rotation that would seriously limit motor efficiency. 

On the other hand, when elastic deformation occurs through a repulsive force mediated by the solvent, as would be the interpretation of the consilient mechanism for the elastic deformation reported by Menz et al., then dissipation through a lattice of chains would be limited and a high efficiency could be expected. The... 

Hypothesis Efficient Production of Motion by Muscle Contraction Derives from the Hydrophobic and Elastic Consilient Mechanisms, Whereby Dephosphorylation Results in Hydrophobic Association Coupled to Near-ideal Elastic Force Development... 

The above perspectives are natural consequences of both the hydrophobic and the elastic consilient mechanisms as applied to the structural data on the myosin II motor. Here we briefly explore the elastic element. An ideal elastomer exhibits exactly reversible stress-strain curves with complete recovery on relaxation of the energy of deformation. On the other hand, an elastomer that exhibits hysteresis does not recover all of the energy on relaxation that was expended on deformation. Accordingly, efficient muscle contraction should involve the deformation of near-ideal elastic segments to utilize more efficiently the energy expended in driving contraction. The mechanism of elasticity that can provide such near-ideal elasticity is the damping of internal chain dynamics on extension. 

E.2.9 The Elastic Consilient Mechanism as the Efficient Mechanical Coupler Within the Vital Force ... 

Elastic forces come into play as hydrophobic associations stretch interconnecting chain segments. Only if the elastic deformation is ideal does all of the energy of deformation become recovered on relaxation. To the extent that hysteresis occurs in the elastic deformation/ relaxation, energy is lost and the protein-based machine loses efficiency. Thus, the elastic consilient mechanism, whereby the force-extension curve can be found to overlay the force-relaxation curve becomes the efficient mechanical coupler within the vital force. The objective now becomes one of understanding the age-old problem of a reluctance to discard past idols. 

E.2.9.3 Bursts of Apolar-Polar Repulsive Free Energy on Hydrolysis of ATP, by the Hydrophobic Elastic Consilient Mechanism, Can Convert to Elastic Deformation for Efficient Energy Conversion... 

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