Protein folding simple, exact models

Dill K A, Bromberg S, Yue K, Fiebig K M, Yee D P, Thomas P D and Chan H S 1995 Principles of protein folding—a perspective from simple exact models Protein Sci. 561-602... 

KA Dill, S Bromberg, K Yue, KM Fiebig, DP Yee, PD Thomas, HS Chan. Principles of protein folding—A perspective from simple exact models. Protein Sci 4 561-602, 1995. 

All these studies seem to indicate that the cooperativity of the folding process is due to the specific pattern of tertiary interactions and/or the specific interplay between short- and long-range interactions. This may appear to be a trivial statement, but detailed analysis of the results from the simple, exact model, protein-like models and reduced models of real proteins show several specific requirements for the protein folding cooperativity. It is very encouraging that over the entire spectrum of theoretical model studies of the protein folding process, these requirements essentially overlap [35-37,51,83,92,95]. Naturally, various models place different stress on the specific interactions that may control protein folding and structural uniqueness. 

Protein Sci., 4, 561 (1995). Principles of Protein Folding-a Perspective from Simple Exact Models. 

Dill, K.A., Bromberg, S., Yue, K., Fiebig, K.M., Yee, D.P., Thomas, P.D., Chan, H.S., 1995. Principles of protein folding-a perspective from simple exact models. Protein Science A Publication of the Protein Society 4 (4), 561. 

The two-dimensional square lattice protein folding model discussed earlier provides a simple basis for probing this issue. The model has the advantage of allowing one to carry out many exact calculations to check the predictions from first-order sensitivity theory. Unlike molecular dynamics or Monte Carlo simulations, there are no statistical errors or convergence problems associated with the calculations of the properties, and their parametric derivatives, of a model polypeptide on a two-dimensional square lattice. 

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