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Biochemical Reactions - Vibrating proteins

slo1
Posts: 4,353
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6/3/2014 12:55:13 PM
Posted: 2 years ago
http://www.sciencedaily.com...

Afar back as 1948, Erwin Schr"dinger -- the inventor of modern quantum mechanics -- published the book "What is life?"
In it, he suggested that quantum mechanics and coherent ringing might be at the basis of all biochemical reactions. At the time, this idea never found wide acceptance because it was generally assumed that vibrations in protein molecules would be too rapidly damped.

Now, scientists at the University of Glasgow have demonstrated he was on the right track after all.

Using modern laser spectroscopy, the scientists have been able to measure the vibrational spectrum of the enzyme lysozyme, a protein that fights off bacteria. They discovered that this enzyme rings like a bell with a frequency of a few terahertz or a million-million hertz. Most remarkably, the ringing involves the entire protein, meaning the ringing motion could be responsible for the transfer of energy across proteins.
The experiments show that the ringing motion lasts for only a picosecond or one millionth of a millionth of a second. Biochemical reactions take place on a picosecond timescale and the scientists believe that evolution has optimised enzymes to ring for just the right amount of time. Any shorter, and biochemical reactions would become inefficient as energy is drained from the system too quickly. Any longer and the enzyme would simple oscillate forever: react, unreact, react, unreact, etc. The picosecond ringing time is just perfect for the most efficient reaction.

These tiny motions enable proteins to morph quickly so they can readily bind with other molecules, a process that is necessary for life to perform critical biological functions like absorbing oxygen and repairing cells.

The findings have been published in Nature Communications.

Klaas Wynne, Chair in Chemical Physics at the University of Glasgow said: "This research shows us that proteins have mechanical properties that are highly unexpected and geared towards maximising efficiency. Future work will show whether these mechanical properties can be used to understand the function of complex living systems."
slo1
Posts: 4,353
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6/3/2014 12:58:36 PM
Posted: 2 years ago
We already know that proteins have to be folded in recognizable patterns to bind with other molecules and now vibrations may play a role in it as well.

Waaay too early to speculate, but would be interesting if the protein build up such as the plaque involved in Alzheimer could be broken up with vibrations.
Envisage
Posts: 3,646
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6/3/2014 4:05:51 PM
Posted: 2 years ago
At 6/3/2014 12:55:13 PM, slo1 wrote:
http://www.sciencedaily.com...

Afar back as 1948, Erwin Schr"dinger -- the inventor of modern quantum mechanics -- published the book "What is life?"
In it, he suggested that quantum mechanics and coherent ringing might be at the basis of all biochemical reactions. At the time, this idea never found wide acceptance because it was generally assumed that vibrations in protein molecules would be too rapidly damped.

Now, scientists at the University of Glasgow have demonstrated he was on the right track after all.

Using modern laser spectroscopy, the scientists have been able to measure the vibrational spectrum of the enzyme lysozyme, a protein that fights off bacteria. They discovered that this enzyme rings like a bell with a frequency of a few terahertz or a million-million hertz. Most remarkably, the ringing involves the entire protein, meaning the ringing motion could be responsible for the transfer of energy across proteins.
The experiments show that the ringing motion lasts for only a picosecond or one millionth of a millionth of a second. Biochemical reactions take place on a picosecond timescale and the scientists believe that evolution has optimised enzymes to ring for just the right amount of time. Any shorter, and biochemical reactions would become inefficient as energy is drained from the system too quickly. Any longer and the enzyme would simple oscillate forever: react, unreact, react, unreact, etc. The picosecond ringing time is just perfect for the most efficient reaction.

These tiny motions enable proteins to morph quickly so they can readily bind with other molecules, a process that is necessary for life to perform critical biological functions like absorbing oxygen and repairing cells.

The findings have been published in Nature Communications.

Klaas Wynne, Chair in Chemical Physics at the University of Glasgow said: "This research shows us that proteins have mechanical properties that are highly unexpected and geared towards maximising efficiency. Future work will show whether these mechanical properties can be used to understand the function of complex living systems."


This is really cool stuff. I wonder which proteins are highly optimised for such interactions, myoglobin? It seems that these interactions will depend heavily on the mass of the protein, and it's tertiary bonding.

I also wonder if these effects are also important at even smaller scales, in industrial chemistry. Fact is we just don't know all the mechanistic details of even some of the 'simple' reactions, let alone ones involving comparatively enormous protein molecules.