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Philip Cunningham: Darwinian Materialism vs. Quantum Biology – Part II

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Notes.

See also: From Philip Cunningham: Darwinian Materialism Vs Quantum Biology

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Here are a few more factoids, besides Quantum coherence, that show us that cells are far more 'in tune' with vibrations. than the simplistic model of cells being dominated by random noise, that Darwinists would apparently prefer people to believe:
Symphony of Life, Revealed: New Imaging Technique Captures Vibrations of Proteins, Tiny Motions Critical to Human Life - Jan. 16, 2014 Excerpt: To observe the protein vibrations, Markelz' team relied on an interesting characteristic of proteins: The fact that they vibrate at the same frequency as the light they absorb. This is analogous to the way wine glasses tremble and shatter when a singer hits exactly the right note. Markelz explained: Wine glasses vibrate because they are absorbing the energy of sound waves, and the shape of a glass determines what pitches of sound it can absorb. Similarly, proteins with different structures will absorb and vibrate in response to light of different frequencies. So, to study vibrations in lysozyme, Markelz and her colleagues exposed a sample to light of different frequencies and polarizations, and measured the types of light the protein absorbed. This technique, , allowed the team to identify which sections of the protein vibrated under normal biological conditions. The researchers were also able to see that the vibrations endured over time, challenging existing assumptions. "If you tap on a bell, it rings for some time, and with a sound that is specific to the bell. This is how the proteins behave," Markelz said. "Many scientists have previously thought a protein is more like a wet sponge than a bell: If you tap on a wet sponge, you don't get any sustained sound." http://www.sciencedaily.com/releases/2014/01/140116084838.htm The Puzzling Role Of Biophotons In The Brain - Dec. 17, 2010 Excerpt: In recent years, a growing body of evidence shows that photons play an important role in the basic functioning of cells. Most of this evidence comes from turning the lights off and counting the number of photons that cells produce. It turns out, much to many people’s surprise, that many cells, perhaps even most, emit light as they work. In fact, it looks very much as if many cells use light to communicate. There’s certainly evidence that bacteria, plants and even kidney cells communicate in this way. Various groups have even shown that rats brains are literally alight thanks to the photons produced by neurons as they work.,,, ,,, earlier this year, one group showed that spinal neurons in rats can actually conduct light. ,, Rahnama and co point out that neurons contain many light sensitive molecules, such as porphyrin rings, flavinic, pyridinic rings, lipid chromophores and aromatic amino acids. In particular, mitochondria, the machines inside cells which produce energy, contain several prominent chromophores. The presence of light sensitive molecules makes it hard to imagine how they might not be not influenced by biophotons.,,, They go on to suggest that the light channelled by microtubules can help to co-ordinate activities in different parts of the brain. It’s certainly true that electrical activity in the brain is synchronised over distances that cannot be easily explained. Electrical signals travel too slowly to do this job, so something else must be at work.,,, (So) It’s a big jump to assume that photons do this job. http://www.technologyreview.com/view/422069/the-puzzling-role-of-biophotons-in-the-brain/
bornagain77
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Besides, as was shown in the video, the quantum coherence of proteins severely muffling the random background noise in the cell, here is another reason why we should consider the noise in the cell to be exceptionally suppressed. Bruce Alberts states the reason why it seemed reasonable in the 1960's for them to consider the cell to be dominated by randomly colliding protein molecules as such. "Consider an enzyme, for example. If its substrate molecule is present at a concentration of 0.5mM,which is only one substrate molecule for every 105 water molecules, the enzyme’s active site will randomly collide with about 500,000 molecules of substrate per second. And a typical globular protein will be spinning to and fro, turning about various axes at rates corresponding to a million rotations per second.
“We have always underestimated cells. Undoubtedly we still do today. But at least we are no longer as naïve as we were when I was a graduate student in the 1960s. Then, most of us viewed cells as containing a giant set of second-order reactions: molecules A and B were thought to diffuse freely, randomly colliding with each other to produce molecule AB — and likewise for the many other molecules that interact with each other inside a cell. This seemed reasonable because, as we had learned from studying physical chemistry, motions at the scale of molecules are incredibly rapid. Consider an enzyme, for example. If its substrate molecule is present at a concentration of 0.5mM,which is only one substrate molecule for every 105 water molecules, the enzyme’s active site will randomly collide with about 500,000 molecules of substrate per second. And a typical globular protein will be spinning to and fro, turning about various axes at rates corresponding to a million rotations per second. But, as it turns out, we can walk and we can talk because the chemistry that makes life possible is much more elaborate and sophisticated than anything we students had ever considered. Proteins make up most of the dry mass of a cell. But instead of a cell dominated by randomly colliding individual protein molecules, we now know that nearly every major process in a cell is carried out by assemblies of 10 or more protein molecules. And, as it carries out its biological functions, each of these protein assemblies interacts with several other large complexes of proteins. Indeed, the entire cell can be viewed as a factory that contains an elaborate network of interlocking assembly lines, each of which is composed of a set of large protein machines.” – Bruce Alberts, “The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists,” Cell, 92 (February 6, 1998): 291-294) https://brucealberts.ucsf.edu/publications/BAPub157.pdf Editor-in-Chief of Science (2009-2013). Dr Alberts served two six-year terms as the president of the National Academy of Sciences
I don't know where Bruce Alberts got his data about water, but we now know that, "When bound to proteins, water molecules participate in a carefully choreographed ballet that permits the proteins to fold into their functional, native states. This delicate dance is essential to life."
Water Is 'Designer Fluid' That Helps Proteins Change Shape - 2008 Excerpt: "When bound to proteins, water molecules participate in a carefully choreographed ballet that permits the proteins to fold into their functional, native states. This delicate dance is essential to life." http://www.sciencedaily.com/releases/2008/08/080806113314.htm
Moreover, "Zhong's group demonstrated that water molecules slow down when they encounter a protein.,,, where the water moved a certain way, the protein folded nanoseconds later, as if the water molecules were nudging the protein into shape."
Scientists glimpse why life can't happen without water - June 20, 2016 Water molecules control protein motion, study finds Excerpt: Water molecules typically flow around each other at picosecond speeds, while proteins fold at nanosecond speeds--1,000 times slower. Previously, Zhong's group demonstrated that water molecules slow down when they encounter a protein. Water molecules are still moving 100 times faster than a protein when they connect with it, however. In the new study, the researchers were able to determine that the water molecules directly touched the protein's "side chains," the portions of the protein molecule that bind and unbind with each other to enable folding and function. The researchers were also able to note the timing of movement in the molecules. Computer simulations at the Ohio Supercomputer Center (OSC) helped the researchers visualize what was going on: where the water moved a certain way, the protein folded nanoseconds later, as if the water molecules were nudging the protein into shape. https://www.sciencedaily.com/releases/2016/06/160620160214.htm
In fact, "WATER'S life-giving properties exist on a knife-edge,,, We are used to the idea that the cosmos’s physical constants are fine-tuned for life. Now it seems water’s quantum forces can be added to this “just right” list."
Water's quantum weirdness makes life possible - October 2011 Excerpt: WATER'S life-giving properties exist on a knife-edge. It turns out that life as we know it relies on a fortuitous, but incredibly delicate, balance of quantum forces.,,, They found that the hydrogen-oxygen bonds were slightly longer than the deuterium-oxygen ones, which is what you would expect if quantum uncertainty was affecting water’s structure. “No one has ever really measured that before,” says Benmore. We are used to the idea that the cosmos’s physical constants are fine-tuned for life. Now it seems water’s quantum forces can be added to this “just right” list. http://www.newscientist.com/article/mg21228354.900-waters-quantum-weirdness-makes-life-possible.html
Thus since Bruce Alberts' initial data on how water acts with proteins was either incomplete or just plain wrong, and we now know that water itself is exceptionally fine tuned for life, then that gives us even more reason to believe there is far less random noise in the cell than was initially thought.bornagain77
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