DIPOLYMERIC MODEL OF PROTEIN FOLDING Frank Potthast "Diplomarbeit" Advisor: Anders Irb\"ack Abstract A dipolymeric chain with fixed bond lengths and continuous bond angles has been implemented in two dimensions. Using the hydrid Monte Carlo algorithm, one observes completely different structural features and different folding characteristics for different residue sequences. Characteristics range from spin-glass type energy landscapes to chains with clearly pronounced minima, the latter having unique native states while allowing for fast folding. Simulating all the 528 chains containing ten residues, it is possible to show that basic needs of a protein, thermodynamic stability and fast folding, can be achieved in this model. February 1995