Moderators: Calilasseia, Mazille
Rumraket:
So in order to understand every step in the evolution of FlglE, you'd have to understand all the other proteins in the flagellar evolution too.
Rumraket:
The existence of protein homologues are a testable prediction of evolutionary theory
Pierre Paul-Grassé:
In sum the mutations of bacteria and viruses are merely hereditary fluctuations around a median position; a swing to the right, a swing to the left, but no final evolutionary effect.
I wrote:
Steps of single amino acid changes along the path are not going to result in a functional protein for every step.
Rumraket:
Are you implying that the changes are going to result in a protein with loss of function, or simply that the change was neutral and therefore did not result in increased functionality? In addition, I'd like to know how you know this?
Rumraket:
So you did those supercomputermodelings? Fascinating. Please share your results.
I wrote:
A few evolutionary facts have been given which I presume are supposed to argue against my position. The ones I can recall are:
A monkeyflower turning into a monkeyflower, a peppered moth turning into a peppered moth and hydrogen producing bacteria turning into hydrogen producing bacteria. I have no problem with these examples of evolution.
Rumraket:
Hahaha... the micro/macro evolution canard.
And you are arguing against a bacteria without a flagellum evolving into a bacteria with a flagellum? Great. Sounds like a double standard to me.

I wrote:
A few evolutionary facts have been given which I presume are supposed to argue against my position. The ones I can recall are:
A monkeyflower turning into a monkeyflower, a peppered moth turning into a peppered moth and hydrogen producing bacteria turning into hydrogen producing bacteria. I have no problem with these examples of evolution.
Calilasseia:
This is merely the wholly absurd regurgitation of the "I've never seen a cat give birth to a dog" piece of creationist scientific illiteracy. Which, apart from being scientifically illiterate, is a duplicitous strawman caricature of evolutionary theory erected for mendacious apologetic purposes.

CharlieM wrote:Quite right, tinkering with one protein on the path affects the whole system. Its a bit like a Rubic cube only vastly more complicated. I'd say beyond the capabilities of unguided forces.
CharlieM wrote:Protein homologues give us a clue that the proteins are related and were possibly derived from the same source. I have been told constantly that the path is too complex to work out. So how do we know that naturalistic evolution is the means by which the path is crossed or is even capable of negotiating that path?
CharlieM wrote:Must I just take it on faith? Just because we observe mutations/duplications/shufflings does not mean that they are unguided.
CharlieM wrote:If DNA replication is the result of an accident where did the error correcting mechanism come from?
Abstract
We describe compartmentalized self-replication (CSR), a strategy for the directed evolution of enzymes, especially olymerases. CSR is based on a simple feedback loop consisting of a polymerase that replicates only its own encoding gene. Compartmentalization serves to isolate individual self-replication reactions from each other. In such a system, adaptive gains directly (and proportionally) translate into genetic amplification of the encoding gene. CSR has applications in the evolution of polymerases with novel and useful properties. By using three cycles of CSR, we obtained variants of Taq DNA polymerase with 11-fold higher thermostability than the wild-type enzyme or with a >130-fold increased resistance to the potent inhibitor heparin. Insertion of an extra stage into the CSR cycle before the polymerase reaction allows its application to enzymes other than polymerases. We show that nucleoside diphosphate kinase and Taq polymerase can form such a cooperative CSR cycle based on reciprocal catalysis, whereby nucleoside diphosphate kinase produces the substrates required for the replication of its own gene. We also find that in CSR the polymerase genes themselves evolve toward more efficient replication. Thus, polymerase genes and their encoded polypeptides cooperate to maximize postselection copy number. CSR should prove useful for the directed evolution of enzymes, particularly DNA or RNA polymerases, as well as for the design and study of in vitro self-replicating systems mimicking prebiotic evolution and viral replication.
CharlieM wrote:Pierre Paul-Grassé:
In sum the mutations of bacteria and viruses are merely hereditary fluctuations around a median position; a swing to the right, a swing to the left, but no final evolutionary effect.
CharlieM wrote:The amino acid sequence of FlgE is far longer than its homologs and so gene duplication and joining is the proposed path in its development. This involves more than a single step so I'd be surprised if anyone believed that a sequence of functional proteins in single steps occurred.
CharlieM wrote:Well Matzke proposed the path so ask him. Although the search space that naturalistic evolution needs to sample is so large that it would indeed take a supercomputer to find a way through.
CharlieM wrote:Why? With the flagellum we have a novel structure with a new function, with the others we don't, unless you want to stretch the definition of, "function".
CharlieM wrote:And besides that is not what I'm arguing against.
CharlieM wrote:Not exactly. This is the evidence I have been presented with. This to me only demonstrates the plasticity of types to adapt to their environment.
CharlieM wrote:I have no problem with humanity emerging through all the forms from a single cell to what we are today, so if you presented me with solid evidence that we were once aquatic, fish-like beings, I'd say, well done, but it doesn't affect the way I envision evolution happening.

CharlieM wrote:Rumraket:
So in order to understand every step in the evolution of FlglE, you'd have to understand all the other proteins in the flagellar evolution too.
Quite right, tinkering with one protein on the path affects the whole system. Its a bit like a Rubic cube only vastly more complicated. I'd say beyond the capabilities of unguided forces.

! |
MODNOTE This post and a few of its replies were merged from this thread: "Creationists Read This". -Mr.Samsa |
Excerpt from http://www.discovery.org/a/1831
In a recent column in the Wall Street Journal (February 13, 2004, Science Journal, page B1, "Evolution Critics Come Under Fire for Flaws In 'Intelligent Design'") science writer Sharon Begley repeated some false claims about the concept of irreducible complexity (IC) that have been made by Darwinists, in particular by Kenneth Miller, a professor of biology at Brown University. After giving a serviceable description in her column of why I argue that a mousetrap is IC, Begley added the Darwinist poison pill to the concept. The key misleading assertion in the article is the following: "Moreover, the individual parts of complex structures supposedly serve no function." In other words, opponents of design want to assert that if the individual parts of a putatively IC structure can be used for anything at all other than their role in the system under consideration, then the system itself is not IC. So, for example, Kenneth Miller has seriously argued that a part of a mousetrap could be used as a paperweight, so not even a mousetrap is IC. Now, anything that has mass could be used as a paperweight. Thus by Miller's tendentious reasoning any part of any system at all has a separate "function". Presto! There is no such thing as irreducible complexity.
That's what often happens when people who are adamantly opposed to an idea publicize their own definitions of its key terms—the terms are manipulated to wage a PR battle. The evident purpose of Miller and others is to make the concept of IC so brittle that it easily crumbles. However, they are building a straw man. I never wrote that individual parts of an IC system couldn't be used for any other purpose. (That would be silly—who would ever claim that a part of a mousetrap couldn't be used as a paperweight, or a decoration, or a blunt weapon?) Quite the opposite, I clearly wrote in Darwin's Black Box that even if the individual parts had their own functions, that still does not account for the irreducible complexity of the system. In fact, it would most likely exacerbate the problem, as I stated when considering whether parts lying around a garage could be used to make a mousetrap without intelligent intervention.
In order to catch a mouse, a mousetrap needs a platform, spring, hammer, holding bar, and catch. Now, suppose you wanted to make a mousetrap. In your garage you might have a piece of wood from an old Popsicle stick (for the platform), a spring from an old wind-up clock, a piece of metal (for the hammer) in the form of a crowbar, a darning needle for the holding bar, and a bottle cap that you fancy to use as a catch. But these pieces, even though they have some vague similarity to the pieces of a working mousetrap, in fact are not matched to each other and couldn't form a functioning mousetrap without extensive modification. All the while the modification was going on, they would be unable to work as a mousetrap. The fact that they were used in other roles (as a crowbar, in a clock, etc.) does not help them to be part of a mousetrap. As a matter of fact, their previous functions make them ill-suited for virtually any new role as part of a complex system.
Darwin's Black Box, page 66.
The reason why a separate function for the individual parts does not solve the problem of IC is because IC is concerned with the function of the system:
By irreducibly complex I mean a single system which is composed of several well-matched, interacting parts that contribute to the basic function, and where the removal of any one of the parts causes the system to effectively cease functioning.
Darwin's Black Box, page 39.
The system can have its own function, different from any of the parts. Any individual function of a part does not explain the separate function of the system.

CharlieM wrote:I wish I had more time to participate in this interesting discussion but my internet access will be very limited over the next few weeks. I will try to follow the arguments and, who knows, they may still be going strong when I return.
I still haven't heard any plausible explanation as to how the flagellar universal joint came by its remarkable ability to assemble and rotate in the way it does. I'm seriously interested in finding an answer.
Anyway I will leave this quote from Behe and try to answer any responses to this post if and when I get a chance.


CharlieM wrote:The ten parts that Miller has left are non-functional as a motility system. He has taken forty parts away and the motility system has lost its function. Therefore as a motility system it is non-functional. Why does Miller never acknowledge this?

CharlieM wrote:The ten parts that Miller has left are non-functional as a motility system. He has taken forty parts away and the motility system has lost its function. Therefore as a motility system it is non-functional. Why does Miller never acknowledge this?

CharlieM wrote:I still haven't heard any plausible explanation as to how the flagellar universal joint came by its remarkable ability to assemble and rotate in the way it does. I'm seriously interested in finding an answer.
CharlieM wrote:Anyway I will leave this quote from Behe and try to answer any responses to this post if and when I get a chance.

Rumraket:
That's it. Nothing more to say. The irreducible complexity claim is a strawman because it fails to reckognise that the intermediate steps leading to a finalized flagellum doesn't have to serve a motility function. Any beneficial funcition will do, whatever it's nature. Case closed.
From a paper linked to by GenesForLife:
One part of this claim is that each flagellar component is used solely for the purpose of making a flagellum that, in turn, is used only for motility. Further, each flagellar protein is assumed to have appeared independently of the other component

CharlieM wrote:It does recognize this. Say there are four parts serving different functions. They have to be copied, adapted, produced at the right time and place in the right quantity and interact with each other in a suitable way.
CharlieM wrote:Consider the hook as one of those parts. It is made up of over one hundred protein units formed and assembled on site in a precise manner. It needs to bind accurately to itself and its neighbours and it needs to rotate in a way that is unique and cannot be achieved by unregulated forces from within the protein units.
CharlieM wrote:This is what Behe is saying. You cannot just pick a few systems and throw them together.
CharlieM wrote:There are many other factors to consider. Finding supposed co-opted systems and homologous proteins for some of the parts is not enough.
CharlieM wrote:One thing is for sure, Behe's proposal that the bacterial flagellum is irreducibly complex has stimulated a fair bit of research, which can only be a good thing.From a paper linked to by GenesForLife:
One part of this claim is that each flagellar component is used solely for the purpose of making a flagellum that, in turn, is used only for motility. Further, each flagellar protein is assumed to have appeared independently of the other component
This is another example of misunderstanding Behe's argument.
CharlieM wrote:The reason why a separate function for the individual parts does not solve the problem of IC is because IC is concerned with the function of the system:
By irreducibly complex I mean a single system which is composed of several well-matched, interacting parts that contribute to the basic function, and where the removal of any one of the parts causes the system to effectively cease functioning.
Darwin's Black Box, page 39.


Calilasseia wrote:And of course, Behe's claim that removing parts break the flagellum fatally is refuted by one of the scientific papers I presented in the other thread, where scientists demonstrated experimentally that removing one flagellar gene stopped flagellar biosynthesis, but removing a second gene resulted in flagellar biosynthesis restarting, with the new flagellum functioning as a motility system just as well as the original.
Game. Fucking. Over.

CharlieM wrote:The ten parts that Miller has left are non-functional as a motility system. He has taken forty parts away and the motility system has lost its function. Therefore as a motility system it is non-functional. Why does Miller never acknowledge this?

Domain
D1 has a rather complex, unusual fold composed of many different folding motifs: a stack of four horizontal b-hairpins one above another, alternating their orientations with crossing angles of about 1208 (Asn 79–Leu 115 and Gly 324–Gln 337, on the left side in Fig. 1); a triangular loop (Thr 116–Pro 135, on the right side in front); a four-stranded (Leu 288–Ile 314 and Asn 357–Ser 363) and a two-stranded (Val 315–Asn 321 and Ser 339–Thr 346) b-sheet (in the upper and lower half, respectively, both on the back side); two consecutive b-turns (Thr 346–Phe 352, behind the triangular loop); and a vertically extended chain (Pro 135–Ala 144, in the centre front of the upper half). This extended chain seems to be a backbone around which the other motifs assemble. A three-dimensional structural similarity search using software DALI25 resulted in no match for domain D1, confirming its unique fold. The longest dimensions of domain D1 and D2 are about 50 and 45A ° , respectively, and these two domains are connected along their long axes with an angle of about 708.
As predicted from amino acid sequences and expected from farultraviolet circular dichroic spectra, the structure of FlgE31 is very different from that of the F41 fragment of flagellin21,26, which consists of three domains with domain D1, which consists of three a-helices and a b-hairpin, domain D2, which is formed from many b-hairpins, and domain D3, which is made of a tight b-barrel. It is curious that these two molecules with completely different structures both form the tubular structures with basically the same architecture and helical symmetry.

CharlieM wrote:One thing I don't want to do is get into a Monty Python type argument about IC and things seem to be heading that way. That is why I would prefer to get into more detail and I'm concentrating on the flagellar hook because I see this as possibly the strongest position to argue for the IC of the flagellum. So if anyone can convince me that this is easily explained by unguided natural means, I'm ready to listen.


CharlieM wrote:One thing I don't want to do is get into a Monty Python type argument about IC and things seem to be heading that way. That is why I would prefer to get into more detail and I'm concentrating on the flagellar hook because I see this as possibly the strongest position to argue for the IC of the flagellum. So if anyone can convince me that this is easily explained by unguided natural means, I'm ready to listen.
There is a problem with just saying it has homologs and that's it. Here is a link and an excerpts so that you can see some of the difficulties. It explains one domain of a single hook protein:
http://structbio.vanderbilt.edu/chazin/classnotes/Hybrid-methods-paper1.pdfDomain
D1 has a rather complex, unusual fold composed of many different folding motifs: a stack of four horizontal b-hairpins one above another, alternating their orientations with crossing angles of about 1208 (Asn 79–Leu 115 and Gly 324–Gln 337, on the left side in Fig. 1); a triangular loop (Thr 116–Pro 135, on the right side in front); a four-stranded (Leu 288–Ile 314 and Asn 357–Ser 363) and a two-stranded (Val 315–Asn 321 and Ser 339–Thr 346) b-sheet (in the upper and lower half, respectively, both on the back side); two consecutive b-turns (Thr 346–Phe 352, behind the triangular loop); and a vertically extended chain (Pro 135–Ala 144, in the centre front of the upper half). This extended chain seems to be a backbone around which the other motifs assemble. A three-dimensional structural similarity search using software DALI25 resulted in no match for domain D1, confirming its unique fold. The longest dimensions of domain D1 and D2 are about 50 and 45A ° , respectively, and these two domains are connected along their long axes with an angle of about 708.
As predicted from amino acid sequences and expected from farultraviolet circular dichroic spectra, the structure of FlgE31 is very different from that of the F41 fragment of flagellin21,26, which consists of three domains with domain D1, which consists of three a-helices and a b-hairpin, domain D2, which is formed from many b-hairpins, and domain D3, which is made of a tight b-barrel. It is curious that these two molecules with completely different structures both form the tubular structures with basically the same architecture and helical symmetry.

Shrunk:
Please demonstrate, in precise detail down to the molecular level, the process by which the flagellar hook was "designed".

Return to Evolution & Natural Selection
Users viewing this topic: No registered users and 1 guest