Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 395, Issue 4, Pages 834-843Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.10.044
Keywords
association energy; evolutionary drift; evolutionary selection; surface contact; point group symmetry
Categories
Funding
- Albert-Ludwigs-Universitat
- Wacker Chemie
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The fact that aggregates of identical protein molecules are usually symmetric has remained an enigma. An idealized model of a soluble monomeric protein was constructed and accompanied through a simulated evolutionary process resulting in dimerization, in order to elucidate this peculiarity. The model showed that the probability of a symmetric association is by a factor of 100 or above higher than the probability of an asymmetric one. Unexpectedly, symmetry prevails in the dimer initiation phase much more than in the dimer improvement phase of evolution. The result is clear-cut and robust against a broad spectrum of model inadequacies. It rationalizes the predominance of symmetric homo-oligomers. (C) 2009 Elsevier Ltd. All rights reserved.
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