What’s that doing here?
It is Coyne’s analysis of Lenski’s article in the OP.
My confusion is that I thought it might be intended as a reply to me.
1 Like
Genetic research is not my thing however from what I read ablout this Lenski stuff is that mutations are not random and do not help. Only in special cases did E coli change bodyplan and being from mutations is speculated on. In fact its emphasised that ONLY after a certain number of generations do they have a new food source to greatly increase reproduction.
I don’t see any evolutionary biology claims backed up. in fact it shows it doesn’t work.
There is innate triggers that change things.
Also the changes don’t seem to stick as no new species is created with new scientific names.
Why is this Lenski stuff in any way welcome by evolutionists?? Its a e-flop.
Neutral mutations are only initially neutral. When environmental factors change, what was neutral can become favorable or detrimental.
1 Like
This explanation does not fit the evidence.
Since the obvious response is something you refuse to entertain (that we might want to know WHAT doesn’t fit the evidence), I think I’ll drop out of the discussion at this point.
This is going to be like pulling teeth again…
It simply does not make sense. I used to believe it until I looked at it more closely. The truth is you believe that it could be guided so I think we have common ground here.
Someone did in the comments. Lol. Too predictable
4 Likes
We observe natural mechanisms changing out one base for another. We observe that the difference between two genes in two different species is a base that has been changed out.
Why wouldn’t the naturally occurring and observed mechanism be adequate? It’s as if you are saying that a lottery machine can pick any numbers, but are incapable of picking the winning numbers using the same process.
1 Like
Your homework word for the day is “epistasis”:
Put simply, a neutral mutation today may be a beneficial mutation tomorrow.
4 Likes
Because they still produce changes in things like molecular shape, structure, affinity, size and so on. As long as these changes don’t substantially deleteriously affect an existing adaptive function, such changes can accumulate, and potentially produce new adaptive functions.
They can ever so slightly alter the active site of some enzyme, without negatively affecting it’s function in a substantial way, but having the inadvertent effect of making that active site better able to accommodate another substrate a bit different from the one it was already active on. That’s how for example the lactate dehydrogenases (LDH) enzymes evolved from malate dehydrogenases (MDH).
See: Boucher JI, Jacobowitz JR, Beckett BC, Classen S, Theobald DL. An
atomic-resolution view of neofunctionalization in the evolution of apicomplexan
lactate dehydrogenases. Elife. 2014 Jun 25;3. DOI: 10.7554/eLife.02304
1 Like