In many instances of protein dimerization and protein association/dissociation reactions, multiple hydrogen bonds in close proximity are observed. Such arrangements are also found in protein beta-sheet structures. Even protein helix-coil transitions are driven partly by such nesting of hydrogen bonds. In a well-known model of liquid-liquid phase transition, multiple hydrogen bonds between polymers have also been invoked. In the present study, we attempt to develop a generalized entropy-based theory of polymer association. First, we consider the simple model of two polymer chains. In this model, the free energy change is due to a hydrogen-bond or hydrophobic interaction-induced association is computed by using various theories of polymer statistics. Our study finds an interesting free energy crossover, which gives the number of certain links and spacing between two polymers due to competition between entropic and enthalpic factors. We perform computer simulations of both simple polymer chains and more complex models to explore the equilibrium aspects. Further, we extend this model to understand beta-sheet formation, dimerization of two proteins and polymer chains and formation of liquid droplet through polymer association.

Towards the development of an entropy-based theory of polymer association with relevance to liquid droplet formation

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