Pressure-dependent transition in protein dynamics at about revealed by molecular dynamics simulation.
Molecular dynamics simulations of a crystalline protein, Staphylococcal nuclease, over the pressure range 1 bar to 15 kbar reveal a qualitative change in the internal protein motions at approximately 4 kbar. This change involves the existence of two linear regimes in the mean-square displacement for internal protein motion, <mu2>(P) with a twofold decrease in the slope for P>4 kbar. The major effect of pressure on the dynamics is a loss, with increasing pressure of large amplitude, collective protein modes below 2 THz effective frequency, accompanied by restriction of large-scale solvent translational motion.
Computational Molecular Biophysics, Interdisciplinary Center for Scientific Computing (IWR), University of Heidelberg, Im Neuenheimer Feld 368, D-69120 Heidelberg, Germany.
Lars
L
Meinhold
Jeremy C
JC
Smith
D003198:Computer Simulation; D007700:Kinetics; D008836:Micrococcal Nuclease / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D011312:Pressure; D011487:Protein Conformation
D008836:Micrococcal Nuclease