The Stochastic Evolution of Catalysts in Spatially Resolved Molecular Systems
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J.S. McCaskill
Abstract
A fully stochastic chemical modelling technique is derived which describes the influence of spatial separation and discrete population size on the evolutionary stability of coupled amplification in biopolymers. The model is analytically tractable for an dimensional space (simplex geometry), which also provides insight into evolution in normal Euclidean space. The results are compared with stochastic simulations describing the coevolution of combinatorial families of molecular sequences both in the simplex geometry and in lower (one, two and three) space dimensions. They demonstrate analytically the generic limits which exploitation place on coevolving multicomponent amplification systems. In particular, there is an optimal diffusion (or migration) coefficient for cooperative amplification and minimal and maximal threshold values for stable cooperation. Over a bounded range of diffusion rates, the model also exhibits stable limit cycles. Furthermore, the cooperatively coupled system has a maximum tolerable error rate at intermediate rates of diffusion. A tractable model is thereby established which demonstrates that spatial effects can stabilize catalytic biological information. The analytic behaviour in dimensional simplex space is seen to provide a reasonable guide to the spatial dependence of the error threshold in physical space. Nanoscale possibilities for the evolution of catalysis on the basis of the model are outlined. We denote the modelling technique by PRESS, Probability Reduced Evolution of Spatiallydiscrete Species.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Highlight: Evolution in Vivo, in Vitro and in Machina
- Modeling Genetic Networks and Their Evolution: A Complex Dynamical Systems Perspective
- Evolution in Silico and in Vitro: The RNA Model
- Divergent Evolution of (??)8-Barrel Enzymes
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- Toward Automated Nucleic Acid Enzyme Selection
- Duocalins: Engineered Ligand-Binding Proteins with Dual Specificity Derived from the Lipocalin Fold
- The Stochastic Evolution of Catalysts in Spatially Resolved Molecular Systems
- Fragment-Based Flexible Ligand Docking by Evolutionary Optimization
- Specific Nucleoprotein Complexes within Adenovirus Capsids
- ERH (Enhancer of Rudimentary Homologue), a Conserved Factor Identical between Frog and Human, Is a Transcriptional Repressor
- Signal Transduction by the Chemokine Receptor CXCR5: Structural Requirements for G Protein Activation Analyzed by Chimeric CXCR1/CXCR5 Molecules
- Arginine-Specific Cysteine Proteinase from Porphyromonas gingivalis as a Convenient Tool in Protein Chemistry
- Chemokine-Induced Secretion of Gelatinase B in Primary Human Monocytes
