| Original Articles |
|
|
|
|
Dynamical Transition of Myoglobin and Cu/Zn Superoxide Dismutase Revealed by Molecular Dynamics Simulation |
| ZHANG Li-Li;ZHANG Jian-Hua;ZHOU Lin-Xiang |
| Surface Physics National Key Laboratory, Department of Physics, Fudan University, Shanghai 200433 |
|
| Cite this article: |
|
ZHANG Li-Li, ZHANG Jian-Hua, ZHOU Lin-Xiang 2002 Chin. Phys. Lett. 19 1788-1791 |
|
|
|
Abstract We have carried out parallel molecular dynamics simulations of
solvated and non-solvated myoglobin and solvated Cu/Zn superoxide dismutase at different temperatures. By analysis of several methods, the simulations reproduce the quasielastic neutron scattering experimental results. Below 200 K these two proteins behave as harmonic solids with essentially only vibrational motion, while above this temperature, there is a striking dynamic transition into anharmonic motion. Moreover, the simulations further show that water molecules play an important role for this dynamical transition. There is no such sharp dynamical transition in non-solvated proteins and the higher the solvate density is, the steeper at transition point the curve of mean square displacement versus temperature will be. The simulations also display that the dynamical transition is a general property for globular protein and this transition temperature is a demarcation of enzyme activity.
|
| Keywords:
31.15.Qg
61.43.Fs
|
|
|
Published: 01 December 2002
|
|
|
|
|
|
|
|
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
