INVESTIGATION OF PROTEIN UNFOLDING AND STABILITY BY COMPUTER-SIMULATION

Structural, dynamic and energetic properties of proteins in solution c an be studied in atomic detail by molecular dynamics computer simulati on. Protein unfolding can be caused by a variety of driving forces ind uced in different ways: increased temperature or pressure, change of s olvent composition, or protein amino acid mutation. The stability and unfolding of four different proteins (bovine pancreatic trypsin inhibi tor, hen egg white lysozyme, the surfactant protein C and the DNA-bind ing domain of the 434 repressor) have been studied by applying the afo re-mentioned driving forces and also to some artificial forces. The re sults give a picture of protein (in)stability and possible unfolding p athways, and are compared to experimental data where possible.