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The rate of a protein's evolution relative to the mutation rate depends on the distribution of fitness effect among mutant sequences.
Theory predicts that the rate of a protein's evolution should be largely unaffected by the payoff function, except through the effect of the payoff function on the optimized expression level.
Selected variations in death rates during a tumor's evolution may be added to the basic model.
We found little correlation between a protein's rate of evolution and the amount of temporal variability of that rate.
A flexibility-based explanation assumes that a site's rate of evolution increases with its dynamical flexibility.
Strikingly, even allowing for crossover rates, both the rate of premeiotic DSBs and of noncrossover recombination events predict a gene's rate of evolution.
It is usually considered that the main structural determinant of a site's rate of evolution is its Relative Solvent Accessibility (RSA).
This supports the idea that regardless of how many protein-protein interactions a protein participates in, each interaction affects the protein's rate of evolution.
Therefore, we postulate as our null model an explicit empirical Flexibility Model according to which a site's rate of evolution depends linearly on its MSF.
We aim to elucidate whether a site's rate of evolution depends on flexibility or mutational stress as measured by MSF and MLmS, respectively.
Over twenty-five yeago ago, a number of authors suggested that a protein's rate of evolution should decrease with the number of molecular interactions in which it participates [ 1- 3].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com