Mammuthus
This from a biochemist? Why the hell would the entire protein need to be complementary to interact? I guess he did not clear this up either? Most protein protein interactions are via specific domains
What makes you say he was trying to make the whole protein complemntary? I'd be surprised if he worked with any more than two single domain proteins?
...hell, they can even be linked by a few disulfide bonds
That's trivial as we all know and crucially not specific. It's not easy to get two proteins to form a complex, disulfide bonds aside. He was clearly trying to do it without disulfides! Using pahge-display we all know it takes tens of billions of attempts.
He's trying to generate high affinity not non-spcific binding!
..sounds like Behe confused proteins with DNA
You clearly should have realized that you are on the wrong track here. Behe IS a biochemist so your thoughts here are utterly impossible!
..not to mention dimers and trimers made up of mutliple copies of the same protein..no need for complementary changes in the DNA...on the other hand, I am sure Phillip Johnson was very impressed
But getting SPECIFIC dimerization is NOT trivial. Of course any hydorphobic protein will dimerise but not *specifically* (for itsself ahead of other hydrophobic proteins) without design or billions of steps. And dimerization is much easier tha ngetting two differnt proteins to bind that don't already do so!
This message has been edited by Tranquility Base, 07-07-2005 09:18 PM