Quantum simulation of ferrocytochrome c.
The dramatic progress in the understanding of the dynamics of biomolecules has been largely fuelled by computer simulations based on the law of classical mechanics. However in some respects biomolecules are at the borders of the domain of applicability of classical mechanics. The role of quantum mechanical effects in biomolecular structure and function is therefore worth investigating. Here we present preliminary results from a quantum simulation of a protein and contrast them with results from full classical simulations. The most significant differences are found in motions of high frequency, such as bond stretching or the torsional oscillation of groups that bear hydrogen atoms. The amplitudes of such motions are significantly increased by the penetration of atoms into classically forbidden regions. These differences will directly influence the rates of such processes as proton and electron transfer.
Zheng
C
C
Department of Chemistry, University of Houston, Texas 77004.
Wong
C F
CF
McCammon
J A
JA
Wolynes
P G
PG
D003574:Cytochrome c Group / Q000378:metabolism; D004579:Electron Transport; D008956:Models, Chemical; D011789:Quantum Theory; D013816:Thermodynamics; D014961:X-Ray Diffraction
D003574:Cytochrome c Group