Elastic protein-based machines hydrophobic association

Due to the struggle to survive under circumstances of limited food supply, organisms evolve to use the most efficient mechanism available to their composition. The most efficient mechanism available to the proteins that sustain Life would seem to be the apolar-polar repulsive free energy of hydration as observed for the inverse temperature transitions for hydrophobic association. The efficiency of designed elastic-contractile protein-based machines and a number of additional properties make designed protein-based materials of substantial promise for the marketplace of the future. 

V in Table 5.5 with 0,2,3,4, and 5 F residues per 30-mer exhibits a systematic nonlinear increase in steepness, that is, in positive cooperativity, and an associated nonlinear increased pKa shift, as plotted in Figure 5.34. The energy required to convert from the COOH state to the COO" state systematically in a supralinear way becomes less and less, as more Phe residues replace Val residues. The energy required to convert from the hydrophobically dissociated state of COO" to the hydrophobically associated (contracted) state of COOH becomes less, as the model protein becomes more hydro-phobic. The elastic-contractile protein-based machine becomes more efficient as it becomes more hydrophobic. The cooperativity of Model Protein iv with a Hill coefficient of 2.6 is similar... 

Even so, crystal structures provide the best snapshots of forces in action. Crystal structures provide an unparalleled opportunity to assess relevance to the major protein-based machines of biology of the free energy transduction so dominantly displayed by elastic-contractile model proteins (as developed in Chapter 5). If the apolar-polar repulsive free energy of hydration, AG.p, the operative component of the Gibbs free energy of hydrophobic association, AGha> is active in ATP synthase, then it should become apparent in these snapshots. 

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. 

As shown in the hexagonal array in Figure 5.22, five different energy inputs can perform mechanical work by the consilient mechanism. The set of elastic-contractile model proteins capable of direct utilization of hydrophobic association for contraction are called protein-based molecular machines of the first kind. These are enumerated below with brief consideration of the reversibility of these machines. 

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