A two-dimensional square-lattice model for the formation of secondary structures in proteins, the hydrogen-bonding model, is extended to include the effects of solvent quality. This is achieved by allowing configuration-dependent nearest-neighbor interactions. The phase diagram is presented and found to have a much richer variety of phases than either the pure hydrogen-bonding self-avoiding walk model or the standard Θ -point model.
|Journal||Physical Review E - Statistical, Nonlinear, and Soft Matter Physics|
|Publication status||Published - 15 Feb 2008|
ASJC Scopus subject areas
- Statistical and Nonlinear Physics
- Statistics and Probability
- Condensed Matter Physics