Several studies have focused on the impact of recombination on the evolution of proteins, particularly in relation to directed evolution experiments [4, 5] . Two major factors have a large influence on the functionality of recombinants proteins. The first is the position of recombination breakpoint (the region where the sequence shifts from that of one parental sequence to the other) relative to the location of genetic polymorphisms within the gene. Recombinants involving a large number of non-synonymous substitutions will in fact have a low probability of being functional [2] . The second factor is the position of the breakpoints in relation to the boundaries of discrete protein folds. Breakpoints near the boundaries of these domains will in general have a smaller impact on protein folding, and hence protein function, than breakpoints occurring within them [3, 6, 7] . Recent work on Begomoviruses corroborated these findings by demonstrating that recombination events found in natural viral populations are significantly less disruptive of protein folding than randomly generated recombinants [8] .