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 mec...

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Bibliographic Details
Published in:Nature (London) 1988-08, Vol.334 (6184), p.726-728
Main Authors: Zheng, Chong, Wong McCammon, Chung F. J. Andrew, Wolynes, Peter G
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Atoms & subatomic particles
Biological and medical sciences
Cellular biology
cytochrome c
Cytochrome c Group - metabolism
Electron Transport
Fundamental and applied biological sciences. Psychology
Hemoproteins
mathematical models
Metalloproteins
Models, Chemical
Molecules
Proteins
Quantum Theory
Thermodynamics
X-Ray Diffraction
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/334726a0