Dynamical Principles in Biological Processes: A Model of Charge Migration in Proteins and DNA

The generalized master equations (GMEs) that contain multiple time scales have been derived quantum mechanically. The GME method has then been applied to a model of charge migration in proteins that invokes the hole hopping between local amino acid sites driven by the torsional motions of the floppy...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2000-08, Vol.97 (18), p.9849-9854
Main Authors: Schlag, E W, Yang, D Y, Sheu, S Y, Selzle, H L, Lin, S H, Rentzepis, P M
Format: Article
Language:English
Subjects:
Amino acids
Approximation
Base Sequence
Biochemistry
Charge transfer
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - metabolism
DNA damage
Electron transfer
Electrons
Experimental results
Models, Biological
Models, Chemical
Nucleic Acid Conformation
Physical Sciences
Protein Conformation
Proteins
Proteins - chemistry
Proteins - metabolism
Quantum mechanics
Quantum Theory
Rotation
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Summary:The generalized master equations (GMEs) that contain multiple time scales have been derived quantum mechanically. The GME method has then been applied to a model of charge migration in proteins that invokes the hole hopping between local amino acid sites driven by the torsional motions of the floppy backbones. This model is then applied to analyze the experimental results for sequence-dependent longrange hole transport in DNA reported by Meggers et al. [Meggers, E., Michel-Beyerle, M. E., & Giese, B. (1998) J. Am. Chem. Soc. 120, 12950-12955]. The model has also been applied to analyze the experimental results of femtosecond dynamics of DNA-mediated electron transfer reported by Zewail and co-workers [Wan, C., Fiebig, T., Kelley, S. O., Treadway, C. R., Barton, J. K. & Zewail, A. H. (1999) Proc. Natl. Acad. Sci. USA 96, 6014-6019]. The initial events in the dynamics of protein folding have begun to attract attention. The GME obtained in this paper will be applicable to this problem.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.140196597