Domain coalescence

Domain coalescence (Karplus and Weaver, 1976) is a possible mechanism for protein folding. Zientara et al. (1980) examined the dependence of the coalescence lifetime on the hydration shell. The lifetime depends on the activation barrier contributed by the shell and the extent of the shell. If domains resemble the native protein in hydration, then the minimal extent of the shell and its fluidity favor coalescence. In passing, one notes that the percolation model may apply to folding the coalescence of domains should be analogous to gelation or to diffusion on a partially filled lattice. 

An optimized bi-continuous periodic structure occurs at the early stage of spinodal decomposition. The small domains coalescence with each other at the later stage, in order to minimize the total interfacial area and thus the total free energy of the system. The structural evolution at the later stage is called Ostwald ripening (Ostwald 1896). According to the Porod law. 

Figure 2.14. Polymer solution with between 4>i and separates into two phases with i and 2. The multiple domains coalesce into two macroscopic phases.

Suppression of domain coalescence in the melt flow regime is one of the most important effects of the interfacial reaction on morphology and morphology development. Simdararaj and Macosko [33] have conducted a careful study of morphology as a function of dispersed phase voliune fraction in reactive and non-reactive blends to discern the influence of the reaction. Figure 5.9 illustrates the dependence of the dispersed phase domain size on the dispersed phase concentration for typical uncompatibilized blends. At dispersed phase concentrations less than about 0.5 wt.% the system is dilute enough that coalescence is insignificant due to the very low frequency of dispersed phase domain... 

Villermaux, J. and Devillon, J.C., 1975. Representation de la coalescence et de la redispersion des domains de segregation dans un fluide par un modele d interaction phenomenologique. In Proceedings of the second international conference of chemical reaction engineering. Amsterdam, pp. Bl-13. 

During a steady-state capillary flow, several shear-induced effects emerge on blend morphology [4-6]. It is, for instance, frequently observed that TLCP domains form a fibrillar structure. The higher the shear rate, the higher the aspect ratio of the TLCP fibrils [7]. It is even possible that fibers coalesce to form platelet or interlayers. 

The remaining three antiparallel /3 structures form a miscellaneous category (see Fig. 84). Lactate dehydrogenase d2 and gene 5 protein each has several two-stranded antiparallel j8 ribbons, but they do not coalesce into any readily described overall pattern. The N-terminal domain of tomato bushy stunt virus protein has a unique /3 structure in which equivalent pieces of chain from three different subunits wrap around a 3-fold axis to form what has been called a /3 annulus (Harrison et ah, 1978). Each of the three chains contributes a short strand segment to each of three three-stranded, interlocking /3 sheets. This domain provides one of the subunit contacts that hold the virus... 

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