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1.  Fitness conferred by replaced amino acids declines with time 
Biology Letters  2012;8(5):825-828.
The fitness landscape of a locus, the array of fitnesses conferred by its alleles, can be affected by allele replacements at other loci, in the presence of epistatic interactions between loci. In a pair of diverging homologous proteins, the initially high probability that an amino acid replacement in one of them will make it more similar to the other declines with time, implying that the fitness landscapes of homologous sites diverge. Here, we use data on within-population non-synonymous polymorphisms and on amino acid replacements between species to study the dynamics, after an amino acid replacement, of the fitness of the ancestral amino acid, and show that selection against its restoration increases with time. This effect can be owing to increase of fitness conferred by the new amino acid occupying the site, and/or to decline of fitness conferred by the replaced amino acid. We show that the fitness conferred by the replaced amino acid rapidly declines, reaching a new lower steady-state level after approximately 20 per cent of amino acids in the protein get replaced. Therefore, amino acid replacements in evolving proteins are routinely involved in negative epistatic interactions with currently absent amino acids, and chisel off the unused parts of the fitness landscape.
doi:10.1098/rsbl.2012.0356
PMCID: PMC3440982  PMID: 22628094
evolution; fitness landscape dynamics; absent allele; reversing replacement; epistatic interactions
2.  Rate and breadth of protein evolution are only weakly correlated 
Biology Direct  2012;7:8.
Background
Evolution at a protein site can be characterized from two different perspectives, by its rate and by the breadth of the set of acceptable amino acids.
Results
There is a weak positive correlation between rates and breadths of evolution, both across individual amino acid sites and across proteins.
Conclusions
Rate and breadth are two distinct, and only weakly correlated, characteristics of protein evolution. The most likely explanation of their positive correlation is heterogeneity of selective constraint, such that less functionally important sites evolve faster and can accept more amino acids.
Reviewers
This article was reviewed by Eugene V. Koonin, Arcady R. Mushegyan, and Eugene I. Shakhnovich.
doi:10.1186/1745-6150-7-8
PMCID: PMC3331848  PMID: 22336199

Results 1-2 (2)