Universal model for α-helix and β-sheet structures in protein

We present a unified potential-energy model that successfully reproduces the hydrogen bonding effect in proteins and can be used to represent well-defined secondary structures, both α-helices and β-sheets. The native structures of the model contain both α-helices and β-sheets and are entirely dependent on the sequence of the modelled protein. The model provides structural insight into the physical mechanism of such problems as structural conversion due to mutation and double native conformations with different α-helix and β-sheet contents.