David Bailey
Member
I do not think the discussion about whether or not frame shift is in play negates the value of Nylonase as evidence for recent new function.
This essay:
Is it easy to get a new protein? A reply to Ann Gauger
goes more in to that.
But again you answer a post with several links to good peer reviewed research, with a post on a ID/creationist blog, run by the Discovery Institute.
My main argument in my previous post did not hinge on Nylonase in any way.
The whole issue here is about which side is staying closer to the science. If you want to decide that the orthodox side is automatically to be preferred, then you need go no further. If you want to understand this at the level of who has most authority, then fine - you have your answer. However, remember that Douglas Ax did research at Cambridge University in the LMB, so he isn't exactly a nobody in his field.
He wants to actually test whether evolution by NS can actually achieve the evolution of proteins - rather than take the concept of evolution by NS as axiomatic. It sure isn't obvious that this is remotely possible, but surely a true scientist would applaud this effort to answer the question decisively.
The core of this is that if a stretch of DNA resulted from a frame shift, it will be basically random at that point - the bases are read 3 at a time, and if you remove one base, the result is read in an utterly different way - in effect you will have jumped to a random point in protein space
Reading your last link, I'd say the situation is pretty confused, and not all the commentators are supportive of his argument. However, this nylonase question was originally raised as a slam dunk reason to believe that functional proteins can be easily be found in 'protein space'. I'd have thought that this must at least be an open question at this time. At one point he says
Well 'may be' isn't very definite!For even if functional sequences are rare, they may be clustered together – in which case, getting from one functional protein to the next won’t be so hard, after all.
It seems to me that more research to determine just how easy it really is to mutate a protein into another one with a different function would be useful. The nylonase example seems too bound up in the history of this particular bug before anyone had a reason to take an interest in it!
The E. coli long-term evolution experiment looks intreesting, but I can't read it immediately - my brain is filling up!
BTW, I often edit a post just after putting it up - it is much easier to read on the forum with all the quotes processed etc - so I usually review my posts and ass extra stuff.
Edit: Thinking about it, the idea that useful proteins are common in protein space, makes you wonder why these need the whole mechanism of a code that codes for 20 different amino acids in exact sequence. I mean I know that from the strict materialist viewpoint one shouldn't talk of needs - but if proteins are easy to find wouldn't you think a rather less extravagant mechanism would have evolved?
David
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