Marty's testable ID hypothesis

[Mercer (John Mercer)]

@Marty

Are you suggesting that someone who is right cannot be arrogant?

Nope. I described a specific case. Why are you pretending that I made some sort of global claim?

@Marty

In addition the authority you attempt to claim for yourself, putting on your lab coat like someone putting on a clerical collar, does not impress.

The evidence seems not to matter to you either. Why is that?

@Marty

Plenty of highly educated people are arrogant, self-important, socially inept, hawking personal agendas, and wrong. You should let your game do the talking. So first, sorry to say it, but get over yourself and stick with the subject.

I am, and note that you are doing anything but.

@Marty

In my initial reply to Dan refusing your offer here, I said it was because you are frequently abusive and nitpicking (if I recall correctly).

Is this an example of you letting your game doing the talking?

@Marty

Your post is a great example so first I will engage with that context. I knew you had cherry picked an example…

Really? You accuse me of cherry-picking, then do not offer a single case that contradicts it? Fascinating.

@Marty

I didn’t really want to play this game of yours partly because it simply takes too long, and partly because I didn’t want to have to say most of this. I hate writing tomes. But I guess I have to.

You could, instead, engage with the scientific method and the cryptic hypothesis you offered, but you’re ranting.

@Marty

Most important, rather than even considering in what way my statement might be true, you have read into my statement a global absolute of epic proportions, a new “scientific design hypothesis” or “testable ID hypothesis.” Why?

Because it’s there, Marty. You built in a false assumption that comes from your design hypothesis–that (try to read carefully here) protein interactions (quaternary structure) regulate catalytic activity POSITIVELY.

Your hypothesis is that these interactions are required to turn catalysis on. It’s just wrong, so it falsifies your tacit design hypothesis. That’s how we humans would design life, but it is rarely available to evolutionary mechanisms. The selective advantage conferred by a new catalytic activity (or range of activities) evolves first, then it is regulated, typically negatively.

Can you see that “negatively” is the polar opposite of “POSITIVELY”?

@Marty

But what utter BS you have claimed I said.

I quoted what you said and responded directly to it.

@Marty

You show no interest in clarifying what I meant or where my statement might be true or have boundaries, but have started this thread with no other purpose than to try humiliate me and cower me into submission.

Or maybe I just don’t want people to spread false claims, based on false assumptions, about how biology actually works in real time.

@Marty

The most important falsehood here is how you have misread one simple sentence to hawk your ID-hating agenda.

You haven’t shown how I misread it, Marty.

@Marty

@Mercer

Why did quaternary structure and catalytic activity disappear from your claim?

What?! It didn’t.

It did:

@Marty

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

Then when I challenged it, you falsely claimed that I was misrepresenting it, while removing the specifics:

@Marty

You are suggesting that the binding site is NOT at a “right” location for the protein to have meaningful function.

I didn’t suggest anything at all about right or wrong locations of binding sites. I challenged something much more fundamental and revealing: your false claim about how those interactions regulate function:

@Mercer

When we design machines, we control them by turning them on. You have unwittingly affirmed that this is an integral part of your design hypothesis by misrepresenting the way that things work in real time.

@Marty

In English, my query is shorthand for what was said before, but negated.

It was not even close to what I wrote. It was a classic straw man.

@Marty

I asked you to clarify your OP claim and show me how my statement is wrong.

And I did, with one of biology’s most-studied examples, myosin.

Your false claim:

@Marty

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

For myosin, eliminating all quaternary structure preserves and enhances catalytic activity. It’s the sort of regulation we expect and observe routinely with the iterative mechanisms of evolution, but not with design.

@Marty

Most people might first try to see in what way my statement could be understood so that it makes sense.

I did. I don’t see how you could miss my point:

@Mercer

When we design machines, we control them by turning them on. You have unwittingly affirmed that this is an integral part of your design hypothesis by misrepresenting the way that biology works in real time.

Do you see anything about locations of binding sites in there?

@Marty

If you are unable to see any truth in it, then either you are not an expert or the axe you are grinding is so important to you that you cannot see past it.

That’s not arrogant at all, right, Marty?

@Marty

Read it again, and ask yourself, “In what ways might this be true?”

None, as a global statement.

@Marty

Now I will talk about my very simple sentence in the original post and engage with the science. What percentage of random bound polypeptide complexes will produce meaningful catalytic activity?

That’s irrelevant to your claim. The falsehood of it is in what quaternary structure does.

@Marty

OK, take the DNA in a cell, and in every gene whose product is part of a protein complex, move every binding site maybe ten amino acids one way or the other.

Irrelevant. The falsehood of your claim is in what you claimed that binding does to catalytic activity.

@Marty

I’m thinking your example might be an exception in this category, an unaffected active site.

I’m thinking that your Culture Warrior mentality is preventing you from reading what I wrote.

We can go to higher-order muscle structure and it gets even worse for your claim. Myosins do not simply transduce ATP hydrolysis to force generation in the much more direct way that your car burns gasoline to turn the crankshaft and wheels.

Can you name even a single protein complex in which the catalytic activity is shared between proteins, in that they have to be interacting for catalysis to occur?

Again, exceptions would be cases in which the interactions are required for catalytic activity. My point is that because you are assuming that these were designed, you are assuming that they are designed in the way that you might design them–to turn on. Evolution, as a rule (although there are certain to be rare exceptions) doesn’t have that option.

@Marty

So fundamentally, my sentence is true.

Fundamentally, your sentence is false.

@Marty

Not some grandiose ID hypothesis which you chose to impose on it.

I didn’t impose anything. You made the assumption that quaternary structure is required for enzymatic activity. It has nothing to do with wrong or right binding sites or their locations. Can you name a single case?