It’s just amazing that to support an unsupportable conclusion like ID, people like @colewd have to rewrite the most basic facts, in this case that proteins are sticky, and therefore they precipitate out of solution very easily.
@colewd, can you explain why you are unable to learn and/or acknowledge such a basic, obvious fact?
Because you deny that proteins are sticky. They stick to each other, they stick to themselves. Last night, you were completely unaware of the existence of homodimers.
Not several. Far more. There’s no reason for any of us to repeat his experiments, as there’s no reason to estimate the prevalence of function in sequence space by going backwards, mutating a single temperature-sensitive mutant of a protein and not bothering to assay enzymatic activity, which is a continuous variable.
We don’t need to because we know that we can find beta-lactamase in multiple clones from a library of only 10^8 immunoglobulins.
Now YOU have to explain why Ann Gauger didn’t even know of the existence of the 32-year-old field of catalytic antibodies, and why Axe did not address them in his paper.
No, it’s closer to 70 orders of magnitude.
Yes, it’s a joke. Our own experiments, done for completely different reasons, tell us more than his do.
Why hasn’t Axe repeated his experiment with more enzymes, Bill?
No. How do you defend Axe’s and Gauger’s claims that this single, lousy experiment can be generalized to all proteins?
How many different catalytic antibodies have been found in the mammalian Ig repertoire of only 10^8 in the past 32 years, Bill?