KCS

Quantitative prediction of the possible secondary structures is important to understand the function of proteins at the molecular level. One of the most interesting secondary structures, the α-sheet has been received a great attention because it was proposed as the possible intermediate conformation to form the beta-sheet fibrils in the aggregation process. Including the α-sheet conformation, the eight possible secondary was investigated by using the density functional theory and molecular dynamics simulation to estimate the thermodynamic properties of the secondary structures. The relative thermodynamic properties are discussed in terms of the thermodynamic stability, gibb’s free energy, enthalpy, entropy, dipole moment, and the charge separation.