The main point was about the assumption of 2500 amino acids. Of course there’s no such thing as non-folded protein. (Well, a cooked one.) Proteins fold; just happens.
Or perhaps it’s only that sentence that’s nonsense.
1 Like
There are disordered proteins. Can you get a functional 2500 AA protein without a proper secondary fold including alpha helixes and beta sheets?
Or perhaps your struggling to comprehend the problem.
“your”. 
Teacher Bill is gonna learn us all some good science fer sure!
1 Like
Sure, they’re disordered. But they’re still folded.
Where did you get the number 2500? Why is it special?
That’s it. Blame the victim. You need to try harder to communicate clearly.
2 Likes
PRPF8 is the largest protein in the spliceosome (about 2500 AA’s) which is a unique feature of eukaryotic cells.
You cannot properly represent a combinatorial problem with long sequences on a sheet of paper. A small protein represents a piece of paper the size of the universe with units of measure the size of protons. A protein 10% the size of PRPF8 would be represented by a piece of paper the size of the universe where its island of optimal function maybe the size of a quark.
Why do you assume that it began as a single protein with 2500 AAs?
You are making up a nonsense comparison with no point.
1 Like
That is what we are observing. PRPF8 is a piece of a protein structure that splices out introns from RNA. Within the chemistry of the cell nucleus of a eukaryotic cell this is required to produce MRNA and translate it into proteins. If we knock out this protein the cell will cease to function.
Or you don’t comprehend the point.
Nor does mutating from something at that peak, nor does mutating from something mutated from that peak and selected to be on the edge of thermal stability. That’s what Axe did, and it makes no sense.
Please define the term “secondary fold,” Bill.
It appears to me that you don’t know what you are talking about. You’re just throwing together terms in a way that makes no sense.
No, we are observing that it has 2500AA in whatever taxon you’re looking at right now. THat doesn’t tell you what it looked like in its early evolution.
1 Like
I think it’s a garbled reference to secondary structure.
It seems that you don’t understand the meaning of the term “empirical.”
1 Like
You are right we don’t know but does the simple to complex idea work here? You have a large chicken and egg problem with this protein as it is mission critical to the eukaryotic cell and without it all ready existing the cell cannot self replicate as its introns need to be spliced out. The simple to complex concept of Darwin does not explain its origin.
Sorry, you don’t know that. I believe some of the literature on evolution of the spliceosome has been cited for you, but you always forget this sort of thing right after it’s mentioned.
It is only evidence of limited functional space given a specific starting point. Finding a solution tends to lock that solution in. If you already have a protein for a specific function, and that protein has been optimized over time, then selection will tend to favor that protein over newer proteins that emerge with less optimal function. On top of that, other proteins can evolve that depend on the function of another protein which further locks that protein into place.
Even random proteins will have folds.
How do you determine how many sequences will have activity?
It is only critical in modern eukaryotes. What you need to show is that it has always been critical. You also need to show that this protein is the only possible protein that could have this function, and also show that this function had to evolve. Again, you are painting the bulls eye around the bullet hole.
1 Like
The speculation such as type 2 introns have problems as the chemical make up of the eukaryotic cells nucleus is conditioned so they do not properly function. The chicken and egg problem has not been solved.
You will have to explain what that means.
1 Like