The dominance of symmetry in the evolution of homo-oligomeric proteins.
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.
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstr. 21, 79104 Freiburg im Breisgau, Germany. georg.schulz@ocbc.uni-freiburg.de
Georg E
GE
Schulz
D003198:Computer Simulation; D019143:Evolution, Molecular; D040961:Genetic Drift; D008958:Models, Molecular; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D012641:Selection, Genetic; D013816:Thermodynamics
D011506:Proteins