Polymer-protein association hydrophobicity effect

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. 

Porcar I., Cottet H., Gareil P, Tribet C. Association between protein particles and long amphiphilic polymers effect of the polymer hydrophobicity on binding isotherms. Macromolecules 1999 32(ll) 3922-3929. 

Therefore, TMDSC has been demonstrated to be an effective method to split the overlapping phenomena present in the ITT of elastic protein-based polymers. By tuning the frequency of the periodic component, a maximum split can be achieved that shows an exothermic contribution arising from the Van der Waals contacts attending chain folding and assembly, and an endothermic contribution associated with loss of hydrophobic hydration, the... 

Obviously, the effect of raising the temperature of a loaded, cross-linked elastic band composed of elastic protein-based polymers of the poly(GVGVP) family is to drive hydrophobic association with the consequence of lifting of the attached weight. How does this combine with the above understanding of elasticity to perform mechanical work ... 

Consideration of the effects of stretching begins with hydrophobically associated and cross-linked elastomeric matrix composed of the same protein-based polymer as used in the calorimetry studies with poly[0.8(GVGVP),... 

Early in our studies it was expected that the post-translational modification of proline hydroxylation, so important to proper collagen structure and function, would raise the value of the temperature, T, for the onset of the inverse temperature transition for models of elastin. Accordingly, hydroxyproline (Hyp) was incorporated by chemical synthesis into the basic repeating sequence to give the protein-based polymers poly[fvs,i(Val-Pro-Gly-Val-Gly), fHyp( al-Hyp-Gly-Val-Gly)], where f sl -i- fnyp = 1 and values of fnyp were 0, 0.01, and 0.1. The effect of prolyl hydroxylation is shown in Figure 7.49. Replacement of proline by hydroxyproline markedly raises the temperature for hydrophobic association. Prolyl hydroxylation moves the movable cusp of... 

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