A multicanonical molecular dynamics study for a model protein-g Original Research Article

We have performed the multicanonical molecular dynamics simulation on a simple model protein-g (PDB id: 2gb1). We have treated the protein-g in terms of a model composing only of charged, hydrophobic, and neutral spherical bead-monomers. Since the hydrophobic interaction is considered to have a large effect on protein folding, we particularly focus on the competition between effects of Coulomb interaction and the hydrophobic interaction. We found that the transition from a random coil to compact state is greatly influenced by both parameters and forms of the hydrophobic potential function.