Computer simulation of the dynamics of hydrated protein crystals and its comparison with x-ray data.
The structure and dynamics of the full unit cell of a protein (bovine pancreatic trypsin inhibitor) containing 4 protein molecules and 560 water molecules have been simulated by using the molecular dynamics method. The obtained structure, atom positional fluctuations, and structure factors are compared with x-ray values. A way of calculating the motional contributions to structure factors is proposed.
D000818:Animals; D002417:Cattle; D003201:Computers; D006860:Hydrogen Bonding; D011487:Protein Conformation; D013696:Temperature; D014359:Trypsin Inhibitor, Kazal Pancreatic; D014361:Trypsin Inhibitors; D014867:Water; D014961:X-Ray Diffraction
D014361:Trypsin Inhibitors; D014867:Water; D014359:Trypsin Inhibitor, Kazal Pancreatic