[allmendream]

A protein adapted for heat stress is what I meant and heat stress doesn't equal a heat shock protein. How would epigenetic factors change the protein that the gene coded for to a more heat tolerant enzyme? This must be at least the third time I have asked you this question. How could it?

And the xylenase study i cited was a very good example of exactly what I am talking about, the only thing it is missing was the survey that showed that every possible single base change was attempted during the directed evolution experiment.

[GodGunsGuts]

==How would epigenetic factors change the protein that the gene coded for to a more heat tolerant enzyme?

I have replied with specific examples of how this done. Didn't you read them?

Here's a quote from one of several relevant links I sent you. Does this answer your question, or are you going to keep doing this song and dance in the hopes of dodging the inevitable bullet?:

HSP90 belongs to a class of proteins called chaperones, which help other proteins in the cell fold properly, prevent protein clumping, and escort improperly made proteins to be recycled. These vital functions become even more important when a cell is stressed by heat, cold, toxins or other hardships that affect protein folding.

Hsp90 is particularly interesting because it is specialized to chaperone proteins that are key regulators of growth and development. Thus, it is in a position to couple environmental change to the release of hidden genetic variation and thereby to produce a host of new traits.

http://www.sciencedaily.com/releases/2008/02/080223123054.htm

[GodGunsGuts]

PS I’m still waiting for the study, or at least an article on the same. Why are you having so much trouble finding citations to back up one of your three top examples of Darwinian adaptation?