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Synthetic Molecules Emulate Enzyme Behavior
FiReaNGeL writes "Ohio State University chemists have created a synthetic catalyst that can fold its molecular structure into a specific shape for a specific job, similar to natural catalysts. In tests, the chemists caused the catalysts to twist one way or the other, either to form one chemical product or its mirror image. They confirmed the shape of the molecules at each step using techniques such as nuclear magnetic resonance spectroscopy. Being able to quickly produce a catalyst of a particular shape would be a boon for the pharmaceutical and chemical industries."
maybe it'll finally be cheap enough to ~cure~ things rather than just treat 'em.
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It would be the holy grail. Things like converting glucose to ATP in the body achieve ~70% efficiency. This is absolutely insane. If the scientists could accurately model and design the tertiary structure of proteins at will then they could do things like making ethanol factories using minimal energy. This is extremely significant.
Anyone remember catalytic antibodies - from 20 years ago - which also promised rapid engineering of "enzymes" for specific reactions. They were made by immunizing an animal with a transition state analog - under the theory that stabilizing the transition state would speed up reactions (since that is what enzymes do). Well, these "abzymes" completely revolutionized enzymology and biotechnology.....oh, wait...
Super-powered beef cows. No hormones added.
What's the value of information that you don't know?
How about a catalyst that takes CO2, H2O and photon energy and converts it into sugar and oxygen? Then we could use another catalyst to convert the sugar into alcohol. *Runs off to the patent office*
Women are like electronics: you don't know how damaged they are until you try to turn them on.
That's what the Ohio State chemists find most exciting: the molecule does not maintain only one shape.
See, that's how I'm different. They lost me at the Rockettes.
At some level, it was only a matter of time: put the molecules together in the right order, and (generally) the form the right shape when left to fold by themselves.
But synthesis of enzymes and such has interesting ramifications for medicine (can't think of any enzyme-deficient diseases off the top of my head, but there must be some)
Now what would be *really* interesting is if they could do proteins in general. That would open up a whole world of life-saving drugs.
I have developed a truly marvelous proof of this comment, which this signature is too narrow to contain.
IANAC, but TFA seems to overstate the find and contains several misleading statements.
First, they cannot "quickly produce a catalyst of a particular shape," but rather they are able to take one molecule and make it twist into either of two orientations. This isn't the holy grail of catalyst molecular engineering (to "give scientists a quick and easy way to get the catalyst that they want"); rather, it gives scientists a couple 'bonus' molecular shapes for each catalyst they synthesize. There is no indication that the ability to twist synthetic molecules means that scientists will have a significantly easier time discovering new catalysts that conform to the necessary shape. As TFA says, "[d]espite decades of research, scientists aren't sure exactly how this kind of propagation works." Why should searching for "a catalyst of a particular shape or function," involve any less trial and error than before?
Moreover, the scientists claim that "as long as there is even a slight chemical preference for one of the hands. . . . [t]he 'flexible glove' will find a way to make a better fit, and so it will assist in specifically making one of the mirror image forms." Yet there is no proof that this "chemical preference" necessarily results in the ideal molecular arrangement of the catalyst. In fact, trying to synthesize a molecule that is capable of folding into multiple useful shapes in response to specific chemical environments seems more difficult than synthesizing individual catalysts to each handle one function independently.
Again, I could be wrong, but I think this is only a very preliminary step in making more advanced synthetic catalysts, and not necessarily a way to design them faster.
Flamebait?! Are you people kidding me?! That was a Homer Simpson quote! For the freaking love of Pete. Look, here's what was written:
"They confirmed the shape of the molecules at each step using techniques such as nuclear magnetic resonance spectroscopy."
Good freaking grief people. Get a sense of humor.
Natural catalysts, such as enzymes in the human body that help us digest food, get around this problem by shape-shifting to suit the task at hand. (...)
Natural catalysts reconfigure themselves over and over again in response to different chemical cues -- as enzymes do in the body, for example.
Actually enzymes do a have a somewhat *fixed* fold for a specific (type of) reaction and don't just catalyse this then that etc. They can be highly selective for only one substance / functional chemical group or not. However they certainly don't reconfigure themselves (we're not talking about allosteric enzymes). The cell just produces a different set of enzymes to adjust to new conditions.
In tests, the chemists caused the catalysts to twist one way or the other, either to form one chemical product or its mirror image.
They better have this working 'error-free'. Having a mixture of both shapes can get you into big trouble (http://en.wikipedia.org/wiki/Thalidomide).
"For many chemical reactions to work, molecules must be able to fit a catalyst like a hand fits a glove," RajanBabu said. "Our synthetic molecules are special because they're flexible. It doesn't matter if the hand is a small hand or a big hand, the 'glove' will change its shape to fit it, as long as there is even a slight chemical preference for one of the hands. The 'flexible glove' will find a way to make a better fit, and so it will assist in specifically making one of the mirror image forms."
I'm not sure this is so good - wouldn't you want them to behave like enzymes aswell, being highly selective? And last but not least there is no comparison offered to *real* enzymes in terms of 'speed' and what kind of reactions besides fatty acid hydrogenation are possible.