Elastic-contractile model protein machines

Synthetic Elastic-contractile Model Protein Machines to Energize Phosphates... 

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. 

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. 

The concept of two distinct but interlinked mechanical processes, expanded here as the coupling of hydrophobic and elastic consilient mechanisms, entered the public domain in the publication of Urry and Parker. Experimental results on elastic-contractile model proteins forged the concept, and the work of Urry and Parker extended the concept to contraction in biology. Unexpected in our examination of the relevance of this perspective to biology was to find the first clear demonstration of the concept in biology in a protein-based machine of the electron transport chain as a transmembrane protein of the inner mitochondrial membrane. Unimaginable was the occurrence of the coupled forces precisely at the nexus at which electron transfer couples to proton pumping. 

Such is our journey of Ionian Enchantment from de novo design of elastic-contractile model protein-based machines to enlightenment at a key juncture of energy conversion within living matter. 

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... 

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