again, from your own article:
"Work with the lambda repressor (Reidhaar-Olson and Sauer, 1990) yielded a “value” for the frequency of functional variants of 1 in 10^63 (roughly) for the 92-mer. Work with chorismate mutase (Taylor et al., PNAS 98, 10596-10601, 2001) gave a value of 1 in 10^24 for the 93 amino acid enzyme. Scaled for a similar size protein, Axe’s work gives a value of 1 in 10^59, which falls within the range established by previous work."
so its not just axe work and other papers give similar result.
First, those referenced papers were reportedly referenced in Axe's paper (you *did* read it didn't you?). Which is why they are specifically discussed in the article I linked.
Second, you appear to have completely ignored the following paragraph (which is what I specifically quoted) which discusses the relative methods for identifying and estimating rates of functional polymers. Here it is again:
Studies such as these involve what Axe calls a “reverse” approach – one starts with known, functional sequences, introduces semi-random mutants, and estimates the size of the functional sequence space from the numbers of “surviving” mutants. Studies involving the “forward” approach can and have been done as well. Briefly, this approach involves the synthesis of collections of random sequences and isolation of functional polymers (e.g., polypeptides or RNAs) from these collections. Historically, these studies have involved rather small oligomers (7-12 or so), owing to technical reasons (this is the size range that can be safely accommodated by the “tools” used). However, a relatively recent development, the so-called “mRNA display” technique, allows one to screen random sequences that are much larger (approaching 100 amino acids in length). What is interesting is that the forward approach typically yields a “success rate” in the 10^-10 to 10^-15 range – one usually need screen between 10^10 -> 10^15 random sequences to identify a functional polymer. This is true even for mRNA display. These numbers are a direct measurement of the proportion of functional sequences in a population of random polymers, and are estimates of the same parameter – density of sequences of minimal function in sequence space – that Axe is after.
(emphasis added)
I suggest re-reading the article I linked and spending some time to try to digest it. It appears you merely skimmed it and consequently missed the entire point the author was making in reference to the experiment Axe performed.
and remember that axe paper is about a single domain.
Not even. Axe's experiment was based specifically on a variant of TEM-1 beta-lactamase. Which is primarily why the gross over-extrapolation of his results to all of molecular biology isn't warranted.
This is also discussed in the article I linked. Here is the relevant quote:
Obviously, from these considerations, we can see that assertions that the tiny base of the “hill” in Figure 3 in any way reflects that of a normal enzyme are not appropriate. On this basis alone, we may conclude that the claims of ID proponents vis-a-vis Axe 2004 are exaggerated and wrong. Axe’s numbers tell us about the apparent isolation of the low-activity variant, but reveal little (nor can it be expected to) about the “isolation” or evolution of TEM-1 penicillinase. (Or any other enzyme, for that matter.)
when many biological systems (like the electric organ) contain many genes. so its not 10^60 but more like 10^200.
This isn't supported in the slightest by Axe's paper or anything else. You're just making this up.