Dembski Responds to Rosenhouse

[Rumraket (Mikkel R.)]

@Marty

@Rumraket , @Faizal_Ali , @Roy , @Mercer
Ya know, you guys might actually have to read the book to understand it. Most of the evolutionary analysis here is based on bad concepts of the arguments. Is that why you’re asking us to summarize it for you?

It looks to me like it’s you guys who read something you don’t really think about or assess critically, you then come here quoting it thinking it somehow settles the matter, and then act flabbergasted when it’s picked apart as the pile of rubbish, handwaving, and mere assertion that it is.

So tell me again, why are we supposed to believe it takes 5-6 amino acid substitutions to produce an efficient protein-protein binding site, and why are we supposed to believe only one out of 20 amino acids at each position confers binding? Are you aware that every single one of those assumptions is an outright demonstrable falsehood. I already cited the literature that shows this.

@Marty

@T_aquaticus

B-cells run the math for us. Out of a few billion random sequences we get tons of protein-protein binding sites. This demonstrates that these binding sites can’t be nearly as rare as Behe claims.

This looks good until you realize antibodies can bind to any spot on an antigen that happens to have a sequence that can act as the complement.

That’s true for any two proteins that bind each other. They really can in principle bind each other anywhere that is sufficiently complementary. And it usually just takes a single mutation for that to happen.

@Marty

For a protein complex, you need the complement at a “right” location so that the resulting quaternary structure has meaningful catalytic activity.

Sorry but now you’re just making additional hurdles up.

First of all you’re assuming that protein-protein binding is only meaningful if it’s a complex of enzymes.
Second, many proteins form complex multimers without being enzymes.
Third, usually enzymes are still enzymes that have substantial catalytic activity even without being part of a complex of multiple proteins, and only some of them are more efficient when they stick together into a larger multi-enzyme complexes.

For others these changes are entirely neutral and seem to have evolved simply as a consequence of chance occurrence of sticky patches on their surface:

A hydrophobic ratchet entrenches molecular complexes

@Marty

Even if you get complementary binding sites, having an active protein complex is far from given. The requirements for protein complexes are many orders of magnitude more stringent than B cells.

[Citation needed]

I invite you to consider the case of the irreducibly complex, gated membrane channel T-URF13 which evolved from non-protein-coding RNA:

From Panda's Thumb: The Evolution of T-URF13: Does Irreducible Complexity Count or Not?

Notable mentions of @Art and @NLENTS. Also relevant to an ongoing discussion in another thread. The Discovery Institute, principal advocate of the Intelligent Design (ID) movement in the US, attempts to invalidate scientific results demonstrating that so-called irreducibly complex (IC) biological traits can evolve naturally. According to the ID protagonist Michael Behe (1996), a system is by definition irreducibly complex if it consists of several specifically interacting components which together produce a function such that the removal of any single component leads to the failure of this function. Most biochemical systems are irreducibly complex in that sense. Since they cannot be less complex without losing their function, unguided natural processes based on random mutations and selection cannot build them up gradually, according to Behe. Instead, multiple coordinated mutations would be required simultaneously .