MOLECULAR MODELING OF HEME PEPTIDES - MOLECULAR-DYNAMICS SIMULATION OF MICROPEROXIDASE

The simulation of the dynamic behavior and of the aggregation of a pep tide containing a heme group (MP11) is performed. The force field term s describing the transition metal come from a newly fitted potential w hich gives the correct heme structure and flexibility. The model of an aggregated state is the dimer of MP11; a possible sixth ligand of the originally pentacoordinated iron of one heme could be either a water molecule or a lysine side chain of the second peptide, but the distanc es to the iron are longer than expected in both cases.