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Journal Article

Coherent dynamics in networks of single protein molecules


Stange,  Pedro
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;


Hess,  Benno
Emeritus Group Prof. Dr. B. Hess, Max Planck Institute for Medical Research, Max Planck Society;

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Lerch, H. P., Stange, P., Mikhailov, A. S., & Hess, B. (2000). Coherent dynamics in networks of single protein molecules. Recent research developments in biophysical chemistry, 1, 41-59. Retrieved from http://cat.inist.fr/?aModele%3DafficheN%26cpsidt%3D14194575.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-F4A6-F
Enzymes are single-molecule catalysts representing chemical protein machines. We show that enzymic reactions in small spatial volumes, characteristic for a living biological cell, may proceed in a special kinetic regime of a molecular network. In this regime the enzymic population behaves like a network of communicating machines. When interactions between the machines are sufficiently intensive, strong correlations between intramolecular dynamics of individual machines in the network can emerge. Thus, mutual synchronization of enzymic turnover cycles develops. The theoretical analysis, which has been performed for allosteric product-activated and product-inhibited reactions, as well for the non-allosteric reactions with substrate loops, show that coherent intramolecular dynamics is a robust phenomenon, which persists even when significant intramolecular fluctuations are present.