Posted: Jul 23, 2010 9:41 am
Rumraket:
You keep piling up gaps in our knowledge as evidence of design.
Not gaps, no. Remember a quote I provided several posts back. Here is an excerpt,
A three-dimensional structural similarity search using software DALI25 resulted in no match for domain D1, confirming its unique fold.
This is the kind of knowledge that is available to us these days. We see a complex structure such as this domain of protein FlgE and we know that this has to be inserted or developed from a similar protein to it and its homologs. It would take lots of mutations to achieve this unless we assume that it arrived fully formed and inserted itself in just the right place. Can random changes search through all the available combinations of forms and eventually hit a form that will do the job. You think yes, I think no, I would say its directed.
Rumraket:
Additionally, the hook protein is a mutated duplication of the rod protein, which is itself already a mutated adhesion protein for structural strength. You are making the mistake of thinking that the hook protein had to accumulate mutations on it's own from something completely unrelated that never had a function as a tubular-shaped structural component.
I still don't think you are getting the universal joint thing.
Its no use just having a structure that is elastic in its longitudinal axis. Think of the hook like a muscle in your body, it can contract but it needs a nerve signal to do so. A protein in the hook won't just expand or contract on its own. It needs a signal or an outside force to do this and this signal or force needs to keep the expansions and contractions in time with the speed of the motor or the tail will be flailing all over the place. This is one more complexity of the system that I would very much like to see an explanation of. So if there are any experts out there with any ideas please share them.