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Evolutionary processes and evolutionary noise at the molecular level. II. A selectionist model for random fixations
Journal of Molecular Evolution
|May 26, 1976
Summary
Protein molecules are functional compromises, not optimal. This model proposes selection coefficients for each function, explaining molecular evolution and supporting a molecular evolutionary clock.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Biochemistry
Background:
- Protein molecules function as compromises due to competing functional demands at different sites.
- Existing models often view proteins as suboptimal, with some functions optimized at the expense of others.
Purpose of the Study:
- To propose a model where protein selection coefficients can be broken down into partial coefficients for individual functions.
- To explain how proteins maintain adaptation through kaleidoscopic changes at variable sites.
- To provide a theoretical basis for a molecular evolutionary clock.
Main Methods:
- Decomposition of selection coefficients into partial coefficients for protein functions.
- Analysis of a selective mechanism promoting primary structure changes at variable sites.
- Integration of internal environmental changes into a constant-environmental selection model.
Main Results:
- Proteins fluctuate around maximal adaptation, with selection acting on individual functions.
- A model is presented where selection occurs without genetic load, leading to multipolymorphism.
- The model provides a theoretical foundation for a molecular evolutionary clock, dependent on functional density.
Conclusions:
- Genetic sufficiency is a more adequate concept than genetic optimality for biological fitness.
- Observed substitution frequencies reflect resistance hierarchies, not just randomness.
- Evolutionary significant substitutions can be identified by monitoring functional density changes.