Observing One Of The Greatest Mysteries

Coming out of the ribosome are chains of amino acids, they fold into these three-dimensional structures where the protein takes on a major role in the life of a cell.  However, a small percentage is so complex that it requires help in order to fold correctly. Designed GroEL+GroES enzymes allows these types of proteins to fold privately in a space which holds 60,000 atomic mass units in size.  Next, a designed “chaperone” device plays a vital role by enhancing the speed by 10 when the folding takes place otherwise it might fall into a “kinetic trap” which could cause major damage within the cell.

“Bacterial cells generally contain multiple, partly redundant chaperone systems that function in preventing the aggregation of newly synthesized and stress-denatured proteins,” the authors said.  “In contrast to all other components of this chaperone network, the chaperonin, GroEL, and its cofactor, GroES, are uniquely essential, forming a specialized nano-compartment for single protein molecules to fold in isolation.” Cell

Scientists at Rice University have been trying to model protein folding on computers.  The scientists make an interesting observation, they say, that “Protein folding is regarded as one of the biggest unsolved problems in biophysics.” The mystery consists of proteins finding their native fold through a maze of wrong folds but somehow it’s accomplished very quickly!  But once done, these folded proteins are the workhorses in the cell, performing all kinds of specialized tasks.

Another article in physorg, “Nearly half of all enzymes require metals to function in catalysing biological reactions” such as photosynthesis, metabolism, and respiration.  Kylie Vincent, of Oxford University’s Department of Chemistry, continued: “Both the metal and the surrounding protein are crucial in tuning the reactivity of metal catalytic centres in enzymes.”  Oxford is keen on watching how metallic enzymes work in order to imitate them.  “There is much that we can learn,” Kylie said.

This could open the door for green fuel cells and other inventions may come from a better understanding of these amazing strings of amino acids that fold ever-so-precisely into the most efficient molecular machines ever witnessed! The various research makes no mention of evolution, they would have a difficult time anyway with this one, for example, why would natural selection create a specialized multi-part precision folding machine like GroEL+GroES, when other mechanisms already exist?

This is not a creation with no propose or direction or thought, rather an intelligently made by God which is driven with purpose and designed with specialized parts that is irreducibly complex!

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8 thoughts on “Observing One Of The Greatest Mysteries

  1. One of the great mysteries: why does MIchael not respond to these outstanding questions still:

    (1) Blog readership numbers ?

    (2) Your qualifications to discuss any scientific subject, in response to the challenge to Olorin.

    (3) A substantive review of Signature in the Cell, promised for August 2009.

    (4) outstanding question from Upson Downes on mitochondrial Eve

  2. Michael, chaperonesw are not a “new diswcovery.” What prompted your post just now?

    Nor are chaperonees especially “cvomplex.”

    “Protein folding is regarded as one of the biggest unsolved problems in biophysics.” The mystery consists of proteins finding their native fold through a maze of wrong folds but somehow it’s accomplished very quickly! But once done, these folded proteins are the workhorses in the cell, performing all kinds of specialized tasks.

    Here goes the argument from ignorance again! “The smartest people in the world don’t understand this. Therefore God.”

    Additionally, your source should have told you that the chaperones don’t always work. In that case, there are structures that destroy misfolded proteins. (Uh-oh. Those must have been created too! No, wait—we understand how they work, so they can’t have been created specially. Too bad.)

    Creationism has two problems with time. Something that today is not understood, and was therefore “created,” might tomorrow be understood, and therefore not created. On the other hand, ID’s “specified complexity” requires a preexisting pattern that is like a human artifact (i.e., an outboard motor for the flagellum); thus, before people knew about the pattern (before 1906 when the outboard was invented), the structure was not designed.

    Please let us know when you have solved this problem: Something that is created/designed at one time might not be/have been created or designed at a different time.

    .

    Moreover, I still want to know why you despise dark matter. What has it ever done to you?

  3. still want you to refute me on what I show about the bacterial flagellum. . . .

    . . . the flagellum IS NOT EVEN IRREDUCIBLE. — G. Kuwajima was able to remove ONE-THIRD of the 497 amino acids from the flagellum, AND IT STILL WORKED PERFECTLY!!!!! . . . Also, we know that the L and the P-rings can be taken away from the flagellum, and it will STILL work. . . .

    Still waiting for a refutation . . . .

    Failure to refute can be taken as an indirect admission.

  4. Krisssmith,

    There is a difference between reducible complexity and irreducible. The Bacterial Flagellum has a universal joint, bushing, stator, rotor, drive shaft, propeller which of course resembles an intelligently designed electric motor made by man. It’s these specialized parts that makes up irreducible complexity. Without one of those specialized parts it’s unable to survive. In other words, the system needs those components to exist before it can function and survive.

  5. Olorin,

    “Michael, chaperonesw are not a “new diswcovery.” What prompted your post just now?” Are you imagining what I say than what I’m saying? You quoted your refutation against yourself. The mystery (rather than discovery) I was referring to of course was “protein folding.”

    “Here goes the argument from ignorance again! “The smartest people in the world don’t understand this. Therefore God.” No, designed engineering in nature confirms God’s Word. Science should be more focus on discovering and learning more about empirical data which is exciting and expanding our knowledge, trying to force into a particular framework is not.

  6. Michael :Krisssmith,
    There is a difference between reducible complexity and irreducible. The Bacterial Flagellum has a universal joint, bushing, stator, rotor, drive shaft, propeller which of course resembles an intelligently designed electric motor made by man. It’s these specialized parts that makes up irreducible complexity. Without one of those specialized parts it’s unable to survive. In other words, the system needs those components to exist before it can function and survive.

    Michael, EVEN when one of the specialized parts, the flagellum can work. IT just takes on a new function. The Type 3 Sycretion System has it’s own function APART FROM THE FLAGELLUM, as well do the other protiens. — That fact alone shows that the flagellum precursors could have evolved, WHICH IS EXACTLY DARWIN PREDICTED in the 6th edition of Origin of Species . . . He predicted that there would be change of function.

    Besides, I believe it was Behe himself that claimed that the flagellum WAS NOT reducible. So, you really fail the challenge.

  7. The mystery consists of proteins finding their native fold through a maze of wrong folds but somehow it’s accomplished very quickly! But once done, these folded proteins are the workhorses in the cell, performing all kinds of specialized tasks.

    Protein folding is a major research effort, and has been for many years. Recent news in Science and other journals indicates that we are well on our way to solving this “mystery.” One thing, however, is known, and has been elucidated in the research—it is the chemical structure of a protein that determines its proper fold, not some magical property of its “code.” Proteins fold to the lowest energy state for their atomic makeup. Like a rock falls to the ground in order to minimize its gravitational potential. Or did you think that God makes rocks fall to the ground?

    There is, however, a complication. Proteins can get stuck on their way to the lowest potential. This is like dropping a ball on a rough surface, where the ball may come to rest in a pocket which is not the lowest one, because it has not enough energy to climb over the wall of the pocket it lands in initially. In the same way, proteins can become misfolded. Even with chaperones, the process is error-prone.

    What happens to these misfolded proteins.? One thing that can happen is that they become prions. You may—or may not—have heard of mad cow disease. Misfolded proteins tend to aggregate into “prions” that damage and even kill cells. Current investigations show that other diseases, previously thought to be unrelated, can also result from misfolded proteins—Alzheimer’s, Creutzfeld-Jakob, Huntington’s, Parkinson’s, emphysema, cystic fibrosis, perhaps even diabetes and cancer. And allergies—because the immune system does not produce antibodies fro these “native’ molecules.

    Chaperones are not required for many proteins to fold correctly—no globular proteins, for example, need them. Most proteins have not only a correct fold, but a fixed sequence in which their various components fold—determined by the positions of their electric charges, their hydrophilic/phobic units, and other chemical properties.

    So does evolution have a chicken-and-egg problem here? Proteins need chaperones, chaperones need proteins? If Michael were not so ignorant in this area, he would know that most chaperones are “heat shock” proteins. That is, they are expressed when an organism is exposed to stress, especially high temperatures. Virtually all organisms, bacteria to humans, carry heat-shock proteins—that is, most chaperones had an evolutionary function entirely aside from their role as chaperones.

    Heat-shock proteins have been known since 1962, and their function as chaperones has been known since the 1980s. In case Michael was thinking that chaperones are a recent discovery.

  8. This week’s Science has a news article on how misfolded proteins cause disease, and some possible interventions. See “Clearing Conformational Disease,” Science 329:154-55 (9 July 2010).

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