Investigation of protein unfolding and stability by computer simulation.
Structural, dynamic and energetic properties of proteins in solution can be studied in atomic detail by molecular dynamics computer simulation. Protein unfolding can be caused by a variety of driving forces induced in different ways: increased temperature or pressure, change of solvent composition, or protein amino acid mutation. The stability and unfolding of four different proteins (bovine pancreatic trypsin inhibitor, hen egg white lysozyme, the surfactant protein C and the DNA-binding domain of the 434 repressor) have been studied by applying the afore-mentioned driving forces and also to some artificial forces. The results give a picture of protein (in)stability and possible unfolding pathways, and are compared to experimental data where possible.
Van Gunsteren
W F
WF
Laboratory of Physical Chemistry, ETH Zürich, Switzerland.
Hünenberger
P H
PH
Kovacs
H
H
Mark
A E
AE
Schiffer
C A
CA
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002645:Chickens; D003198:Computer Simulation; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010194:Pancreatin / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry*; D014361:Trypsin Inhibitors; D014764:Viral Proteins; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
C063367:434-repressor protein, Bacteriophage 434; D010940:Plant Proteins; D012097:Repressor Proteins; D013501:Surface-Active Agents; D014361:Trypsin Inhibitors; D014764:Viral Proteins; D010194:Pancreatin; D000516:alpha-Amylases; D009113:Muramidase