Linoleic Acid: Is This The Key That Unlocks The Quantum Brain?

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Travis

Travis

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Photons were found to collapse at retina, not all the way into brain. Hameroff had to work around this.
How? Did they shine a light through a mouse's optic nerve or something?
 
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Travis

Travis

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I went on a Szent-Györgyi reading spree, because he's got nice articles and also to demonstrate that the concept of conductive proteins is certainly not a new idea. It does seem necessary to account for the speed of nerve conduction and metabolism.
Modern biology is a molecular biology. The rates of most biological reactions are assumed to be limited by the classical concepts of mass action theories applicable to reacting molecules in solution. The main bearers of life are the protein macromolecules, which are often to be found incorporated into membrane structures. This situation would appear to violate the physical basis of classical mass action theories and suggests that the functioning of such structural proteins is controlled at the submolecular level. ―Szent-Györgyi⁽¹⁰⁾
Diffusion in insufficient to account for vision and nerve conduction. The only long-range structures in the body are proteins; so naturally, these must be the conduits of information.
Present biology is a molecular biology. According to it, the main bearers of life are the protein macromolecules with their molecular reactions. One may wonder how such poorly reactive clumsy macromolecules could bring about those subtle biological reactions which characterize life and lend its charm to biology. One may wonder whether these macromolecules are really the main actors of life and whether the main actors are not very much smaller and mobile units, electrons, while the macromolecules themselves are rather the stage than the actors of the drama of life. The problem is whether the electrons of proteins could achieve a greater mobility, lending a subtle reactivity to the protein. ―Szent-Györgyi
⁽⁶⁾
But the globular proteins which diffuse freely in the blood are essentially nonconductive. His experiments with casein showed a very low conductivity:
With a Keithley 600 A electrometer, the resistivities of several casein-methylglyoxal samples were determined to be in the range 44-99 GΩ·m at 295 K. When 200 V were applied across the white casein samples, the steady-state currents attained were less than 0.3 pA, corresponding to resistivity values exceeding 50 TΩ·m. Measured in this way, the resistivity of the casein–methylglyoxal complex was some three orders of magnitude less than that of the white casein under the same atmospheric conditions. ―Szent-Györgyi⁽⁸⁾
These are extremely-high value for resistivity, similar to
rubber, but he was still optimistic. He thought that perhaps the peptide backbone of the protein could be made semiconductive by the addition or removal of electrons, in the manner of ceramic semiconductors. This idea was taken seriously, and mathematical models were developed.⁽¹⁰⁾⁽¹³⁾
It was envisaged that the regular arrangement of peptide linkages in the proteins could result in the existence of electronic energy bands similar to those in elemental semiconductors. Theoretical molecular orbital calculations and experimental studies have supported the validity of this general concept, although it is clear that the energy gap between the so-called valence and conduction bands is too large for pure proteins to act as intrinsic semiconductors. However, this does not preclude the proteins' being able to exhibit a significant extrinsic semiconductivity, through the incorporation of an electron-accepting molecule in their structures, for example. Furthermore, because of the large energy band gap, the action of just one electron acceptor molecule in creating a positively charged "hole" in the protein molecule's valence band could be biologically significant, because there will be no masking effect arising from the intrinsic thermodynamic generation of such charge deficiencies. We wish to report on the electronic properties of one such protein-electron acceptor entity, namely those of the casein–methylglyoxal complex. ―Szent-Györgyi⁽⁹⁾
. Such considerations of the reactivity of living systems led one of us to suggest nearly 40 years ago that the functioning of proteins should be understood by considering their submolecular properties. It was envisaged that one manifestation of such submolecular processes would be the ability of proteins to sustain electrical conductivity. However, as shown by the pioneering studies of Eley, proteins isolated in their pure and dry condition are poor conductors. ―Szent-Györgyi⁽¹⁰⁾
But he had hopes for the longer structural proteins, although it had been conceded that globular proteins were practically nonconductive.
This duality in the nature of proteins has, till now, not been fully appreciated. When I proposed, more than 30 years ago (4), that proteins may be semiconductors, the main and apparently decisive argument against my proposition was that none of the great number of proteins isolated in crystals showed any signs of semiconductivity. It was overlooked that crystalline proteins have to belong to the soluble group and so cannot be expected to be semiconductors. It is the structures that are semiconductors, which cannot be crystallized. ―Szent-Györgyi⁽⁶⁾
However, last year Banga and I found that the proteins building up the solid structure of the cell are fibrous, and that these fibrous molecules as shown by their strong thixotropy, are interconnected by inter- molecular forces. Chloroplasts also contain fibrous proteins. This finding allows us to suppose tentatively that a greater number of molecules may join to form such energy continua, along which energy, viz., excited elec- trons, may travel a certain distance. ―Szent-Györgyi⁽¹⁾
But even structural proteins were shown essentially nonconductive. He was forced to concede:
The energies available are insufficient to raise an electron from the ground state into the conduction band of proteins, the distance between the two being about 3 ev. This is probably the reason why my own suggestion, put forward two decades ago, that proteins act as semiconductors, bore no fruit, and so remained a dead duck. ―Szent-Györgyi⁽⁴⁾
But his work in this area gives great insight into the function of methylglyoxal, since he had proposed that its anticancer effect was due to its ability to modify proteins to the extent of changing their conductivity.
The previous chapter opens the possibility that it might have actually been MG or a closely related ketone-aldehyde that served as acceptor in the electronic desaturation of protein and so might have started up the development and differentiation in the a period. ―Szent-Györgyi⁽⁶⁾
He thought that the increase in protein conductivity with the addition of methylglyoxal was due to a Schiff base with lysine, although he hadn't actually proved this. More likely is through the reaction with arginine in which cyclic imidizoles are formed. These are also flourescent, and have now been well-characterized. They have also been recently shown to exert control on the cell's DNA→RNA transcription. This was done by Thornally.
Our studies demonstrate for the first time that methylglyoxal causes post-translational modification of a coregulator protein and that this modification affects gene expression. ―Thornally⁽¹⁴⁾
This, being the simpler case, may also be the more probable one. It involves the assumption that all the systems concerned have identical receptors for the common chemical signal. ―Szent-Györgyi⁽⁷⁾
These imidizazoles were even isolated; they had been proven to exist. The amount of steps, confirmations, details, and proofs shown in Thornally's article is astonishing.⁽¹⁴⁾

It's likely that Szent-Györgyi made no mention of microtubles simply because they weren't well-characterized then. It was not known during that time that they were filled with fluorescent tryptophan and tyrosine side-chains, a detail that he certainly wouldn't overlook. Albert Szent-Györgyi was also a photochemist, and had spent much time speculating on the role of fluorescent and phosphorescent molecules in the
electron transport chain.
It seems possible that a similar transfer of electrons plays a wider role in the various activities of the cells or the maintenance of their living state. It is still an open question how such a transfer of electrons takes place. ―Szent-Györgyi⁽³⁾
Thus, the problem of energetics narrowed down to the question: How could a chemical potential be translated into a free electronic energy? [...] A tentative answer is suggested by my Fig. 7 in which the energy is released as electronic-free energy, which could emit a photon, or do work of any kind.―Szent-Györgyi⁽⁴⁾
The electrons from photosynthesis must be made to do work. He envisions this as progressive charge transfer from one molecule to the next, with the emission of photons.
So, if an electron were transferred from a third substance to A, filling the empty place, then the electron on B could go on to a fourth molecule, or else, if one electron were taken away from the filled level of B (by transferring it, say, to 0₂), then the electron could drop from the excited level to the empty place on the ground level, emitting a photon, and giving a possible explanation for bioluminescence. ―Szent-Györgyi⁽⁴⁾
Such things are known to occur
in vitro. A charge transfer is not a reduction–oxidation reaction, since it involves the transfer of one electron only—often with the concomitant emission of light, or a photon.
We could go on playing with such ideas and imagine that we add to molecules A and B other substances, say, D, etc., A transferring an electron to B, B transferring from its ground state to the excited level of C, C to D, and so on. Now, if I would feed an electron into the empty place of A and take one out (by means of 02) from D, then all the electrons in the excited levels could shift one place, from B to C and C to D. This leads to a very amusing speculation: a biochemistry without chemistry, because the shift of one electron does not involve any rearrangement within the molecules which simply form a quantum mechanical scaffolding on which the electrons can cascade from molecule to molecule giving off gradually their energy. ―Szent-Györgyi⁽⁴⁾
So he obviously has given some thought to the idea that immobilized resonant rings—such as in tryptophan and tyrosine—on a protein could be responsible for this process. He was well aware of the ability of both of these amino acids to undergo charge transfer reactions and phosphorescence. He had done experiments on this personally.
We observed earlier that there occurred between indoles (serotonin) and FMN (flavinemononucleotides) a strong charge transfer-stronger than what might have been expected if one judged only by the P values of the reactants. ―Szent-Györgyi⁽³⁾
And indoles, such as in serotonin and tryptophan, have a peculiar affinity to accept electrons from the flavin ring.
FMN is (as shown by the Pullmans) a fair acceptor, indole a fair donor. But "fair" is a poor compliment and does not explain such a strong reaction; there must be more to it. ―Szent-Györgyi⁽⁴⁾
For this reason, therefore, a tryptophan solution of proper dilution, upon exposure to an unfiltered ultraviolet lamp, emits a distinct, though weak, violet fluorescence easily observable with the unaided eye. [...] This emission picture changed markedly for the aromatic acids when the solutions were made to 0.5 per cent in glucose prior to freezing. Tyrosine and tryptophan in 10⁻³ molar concentration gave short and prolonged afterglows, respectively. These emissions were of considerable intensity. ―Szent-Györgyi⁽⁹⁾
I think he was right, there must be something more to this. Most biologists are handicapped by the fact they they are taught little about photochemistry.
One of my difficulties with protein chemistry was that I could not imagine how such a protein molecule can "live." Even the most involved protein structural formula looks "stupid," if I may say so. If the atomic structure is only the backbone underlying the common energy levels, the thing becomes more likely. ―Szent-Györgyi⁽¹⁾
I am willing to bet that if he had known of the chemical structure of microtubles, and had seen the histological data as well as those obtained
via X-ray crystallography, he would have recognized immediately that these were the very structure he had been looking for—the only suitable structure for long-range transmission.
While most other branches of biochemistry make rapid progress, these gaps remain unbridged. It looks as if something must be missing from our knowledge and way of thinking without which no progress can be made on these lines. A whole dimension seems to be missing somewhere. ―Szent-Györgyi⁽³⁾
The situation is similar in most other biological processes and pathological conditions, such as the degenerative diseases. This suggests that some very basic information is missing. ―Szent-Györgyi⁽⁵⁾
It's missing on purpose. He had very likely figured-this out later, after doing work with methylglyoxal and cancer.

He has also expressed puzzlement over how the "high-energy phosphate bond" of ATP can be made to do work.
What I was unable to understand was how the interaction of two members of the oxidative chain could create a high-energy P-O-P bond, and how this high-energy P-O-P bond could do work, how it could, for instance, make muscle contract, produce mechanical work in muscle, or electric work in nerve cells. My difficulty was this: a chemical reaction consists in the rearrangement of atoms within the system formed by two molecules, say, A + B ⟶ AB ⟶ C + D. Thermodynamics describes the change in useful energy by a ΔF. But how could a rearrangement, taking place within a closed system, do something useful outside? So, for me, these ΔFs were no more than bookkeeping items, and not currency with which to buy something. ―Szent-Györgyi⁽⁴⁾
And realizes that a diphosphonucleotide, such as NADH, should rightly be considered the fundamental unit of bioenegetics—and not changes of heat and entropy, his "delta effs:" ΔF = ΔH + ΔS
It seems probable to me that surprises may be in store on this line for the student of energy relations, and that the energy of DPNH also may be fed more directly than through ATP into the metastable living structure which has to be maintained. ―Szent-Györgyi⁽⁴⁾
So much was his puzzlemnt over how entropy and enthalpy inside of the phosphodiester could be made to do work on another molecule, he examined the electrical characteristics of ATP: namely, the ability of ATP the participate in charge transfer. This can determined by electron spin resonance.
It is therefore of interest to note that, as has been shown by the Courtauld atomic model, folded configurations of ATP may exist in which the triphosphate group is in close proximity to the adenine. In one of these configurations it may be shown that the triphosphate group fits very neatly on the face of the adenine ring structure. In this folded configuration there may be appreciable overlap between the orbitals of the adenine and the triphosphate moieties. ―Szent-Györgyi⁽¹¹⁾
He had hopes that the extra phosphate in ATP—compared with ADP—would allow the terminal phosphate to curl-over and interact with the adenine ring, but there was little actually evidence of charge transfer.
Several possibilities present themselves for understanding the weakness of the ATP signal. [...]
(5) The signal may be due to a transition metal impurity in the form of a metal-ATP complex. Judging from the procedure for the manufacture of ATP,4 such an impurity would be quite a large one. This possibility, though not likely, cannot be ruled out at present. ―Szent-Györgyi⁽¹¹⁾
Perhaps he was missing magnesium? Adenosine triphosphate does have a peculiar affinity for Mg⁺, and they are commonly thought associated within the body. The complex has even been described as a "chelate."

magnesium–ATP.png click to embiggen

So there is are many other good reasons to believe that biophotons travel inside of microtubules. This idea had the endorsement of Szent-Györgyi, although he didn't have access to the information that we have now. Also, "ultraweak emission" had been found emanating from living cells for centuries. Ray Peat even mentions this is one of his articles.
A Russian embryologist, Alexander Gurwitsch, found that the parts of an organ or embryo could exert their stimulating or organizing influence on other cells even through a piece of glass, and by using different types of filter, he identified ultraweak ultraviolet rays as a medium of communication between cells. F.A. Popp and others are currently studying the integrating functions of ultraweak light signals. Guenter Albrecht-Buehler (who has an interesting website called Cell Intelligence) is investigating the role of pulsed infrared signals in cell communication. ―Peat⁽¹⁷⁾
Electrical fields produced by cells, tissues, and organisms have been shown to influence cellular metabolism and physiology, and to influence growth patterns. Closely associated with cellular electrical fields are fields or gradients of pH and osmolarity, and all of these fields are known to affect the activity of enzymes, and so to create environments or fields of particular chemical concentrations.―Peat⁽¹⁷⁾
Interesting side-note: Albert Szent-Gyorgyi had discovered actin but had been chased-out of Europe by Hitler.
This study led to the discovery of a new protein, which he discovered with I. Banga at the University of Szeged, Hungary. They called it "actin" because it made the inactive myosin act to contract. This discovery has an unusual history. It was never published because just when they were about to publish, Hitler occupied Hungary and Szent-Gyorgyi had to disappear "underground" separated from Banga and science. ―Szent-Györgyi⁽¹²⁾
And he makes a Schrödinger-type connection (and also has an ö-umlaut in his name), by viewing animal metabolism as essentially a reversal of photosynthesis.
We can thus drop these arrows and pull the two sides together, as in Fig. 4, completing the sketch with the main actor, the good old sun, which sends us its photons. Carbohydrate and fat are but a side line; if we leave them off, we have before us the essentials of the energy cycle of life, which consists of electrons being boosted up by photons, and then dropping back to their ground level through the living systems, giving up gradually their excess energy which then drives the living machinery. ―Szent-Györgyi⁽⁴⁾

⁽¹⁾Szent-Gyorgyi, Albert. "Towards a new biochemistry." Science 609 (1941).
⁽²⁾Avery, John, Zoltan Bay, and Albert Szent-Györgyi. "On the energy transfer in biological systems." Proceedings of the National Academy of Sciences 47.11 (1961): 1742-1744.
⁽³⁾Szent-Györgyi, Albert, Irvin Isenberg, and Jane McLaughlin. "Local and π-π Interactions in Charge Transfer." Proceedings of the National Academy of Sciences 47.8 (1961): 1089-1093.
⁽⁴⁾Szent-Györgyi, Albert. "Submolecular biology." Radiation Research Supplement 2 (1960): 4-18.
⁽⁵⁾Szent-Györgyi, Albert. "Bioelectronics." Science 161.3845 (1968): 988-990.
⁽⁶⁾Szent-Györgyi, Albert. "The living state and cancer." Proceedings of the National Academy of Sciences 74.7 (1977): 2844-2847.
⁽⁷⁾Együd, Laszlo G., and A. Szent-Györgyi. "On the regulation of cell division." Proceedings of the National Academy of Sciences 56.1 (1966): 203-207.
⁽⁸⁾Pethig, Ronald, and Albert Szent-Györgyi. "Electronic properties of the casein-methylglyoxal complex." Proceedings of the National Academy of Sciences 74.1 (1977): 226-228.
⁽⁹⁾Steele, Richard H., and Albert Szent-Györgyi. "On excitation of biological substances." Proceedings of the National Academy of Sciences 43.6 (1957): 477-491.
⁽¹⁰⁾Gascoyne, P. R., Ronald Pethig, and A. Szent-Györgyi. "Water structure-dependent charge transport in proteins." Proceedings of the National Academy of Sciences 78.1 (1981): 261-265.
⁽¹¹⁾Isenberg, Irvin, and Albert Szent-Györgyi. "On the electron paramagnetic resonance of adenosine triphosphate." Proceedings of the National Academy of Sciences 45.8 (1959): 1232-1233.
⁽¹²⁾Szent-Gyorgyi, Albert, and Jane A. McLaughlin. "The Living State." Journal of Bioelectricity 2.2-3 (1983): 207-212.
⁽¹³⁾Pullman, Bernard, Michael Kasha, and Albert Szent-Györgyi. "Horizons in biochemistry." (1962).
⁽¹⁴⁾Yao, Dachun, et al. "High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A." Journal of Biological Chemistry 282.42 (2007): 31038-31045.
⁽¹⁵⁾Szent-Gyorgyi, A., L. G. Egyud, and Jane A. McLaughlin. "Keto-aldehydes and cell division." Science 155.Feb 3 (1967): 539-543.
⁽¹⁶⁾Együd, L. G., and A. Szent-Györgyi. "Cell division, SH, ketoaldehydes, and cancer." Proceedings of the National Academy of Sciences 55.2 (1966): 388-393.
⁽¹⁷⁾Peat, Ray. "Adaptive substance, creative regeneration: Mainstream science, repression, and creativity."
 
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meatbag

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Travis

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Okay. It starts off with a well-worded paragraph warning about certain authors who engage in quantum woo and not science.
In the last two decades increasing number of researchers speculates that consciousness, which is often referred to as the last great mystery of science, should have quantum origins. However the amount of literature accumulating on the subject is either bad science or pseudoscience. The word “quantum” is used inappropriately by authors with little understanding of its actual meaning who are mostly interested in making their discourse sound more technical and scientific than it otherwise would be. Moreover, the very same writers have little or no knowledge of neuroscience and as a consequence their “quantum mind” proposals are already wrong at the moment of their conception. ―Georgiev
Good thing this had been written before Massimo Cocchi's article, or else Georgiev might still be recovering from shock‼

But he had actually turned-out to be talking about: Hameroff, 1998; Gao, 2003; and Tuszynski’s Group. He attacks Hameroff first:
One of the statements [by Hameroff] is that microtubule-based cilia/centriole structures are quantum optical devices: “microtubule-based cilia in rods and cones directly detect visual photons and connect with retinal glial cell microtubule via gap junctions”. Though it is eccentric to suppose that microtubule based cilia can capture visual photons and microtubules can act as waveguides to transmit the photons to the cerebral cortex, ―Georgiev
This is be no means eccentric. Technically, light is thought to flow concentrically through microtubules
...it is beyond comprehension why the retinal glia microtubules need to be involved in the process. ―Georgiev
I would assume that this is because they are they are between the microtubules or the rod cell and those of the optic nerve. I'm hesitant to continue since he thinks this is beyond comprehension.

(He makes brief mention of the other theories. Judging by his descriptions, Hameroff's articles are the better ones.)

He assumes that the textbook Waldian photoconduction mechanisms are set in stone; unassailable. These 50 year-old chemical mechanisms form the basis for his theoretical attack against the newer models.
Our eyes see the incoming light photons due to the existent photoreceptors located in the retina. The photoreceptors are responsible for the transduction4 of light into electrical signals, which are then delivered to the brain cortex, where we consciously perceive the visual images.
2.1.1 Photon transduction and signal amplification: The sensory transduction (the conversion of the incoming light into electric signal) takes place in the photoreceptors (rods and cones). It is a three stage process involving (1) photon induced isomerization of a pigment called retinal, subsequent to the absorption of a photon, (2) a biochemical cascade to amplify the incoming signal, and subsequent (3) alteration in the conductance of plasmalemmal cyclic nucleotide-gated (CNG) ion channels permeable for Na⁺ ions (see Figure 1). ―Georgiev
I don't think Gilbert Ling and Ray Peat would agree with this series of events. This depends on "cyclic nucleotide-gated ion channels permeable for Na⁺ ions." This is essentially synonymous with Na⁺/K⁺-GTPase, a membrane pump powered through "high-energy" phosphate heat energy (ΔH). I am willing to bet that Szent-Györgyi would not have like this either, since it depends on multiple stages of diffusion: That of of Na⁺ ions, and that of the glutamate released as a consequence of this.
If this molecule absorbs a photon, it undergoes photoisomerization forming straight chain version, known as all-trans-retinal. Alltrans-retinal unleashes a series of conformational changes in the protein opsin fragment producing metarhodopsin II, which is the activated form of rhodopsin. Most of the conformational changes occur in less than a millisecond, but the last transformation, from metarhodopsin II to metarhodopsin III, requires several minutes to accomplish. ―Georgiev
The term "conformation changes" is a massive cop-out, and commonly used when someone is too unsure, confused, or timid to provide a more detailed chemical mechanism. The explanation that best suits Vitamin A's function is "photobleaching:" Where the
cis–trans isomerization of retinal merely obscures the light, almost like a diffraction grating, decreasing the sensitivity in bright light and increasing it in the dark. In my opinion, this is the primary function of vitamin A in the retina.

Even more stages of rate-limiting diffusion and questionable mechanisms are invoked:
Metarhodopsin II initiates the second stage of phototransduction process via activation of an associated Gt molecule known as transducin. Transducin is a typical G-protein, composed of α, β and γ subunits, which is activated by exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) within its α-subunit. Upon activation the Gt α-subunit is transferred to and activates a phosphodiesterase (PDE) that hydrolyzes cytoplasmic cyclic guanosine monophosphate (cGMP) to guanosine monophosphate (GMP). Reduction in the concentration of cytoplasmic cGMP in the photoreceptor outer segment releases bound cGMP from the cyclic nucleotide-gated (CNG) ion channels. Dissociation of cGMP from the CNG ion channels initiates the final stage in the phototransduction process, the inactivation of the Na⁺ currents through these CNG channels in the photoreceptor outer segment. This complex multistage photochemical process might seem cumbersome, ―Georgiev
Cumbersome is an understatement. It's amazing that we can see at all.
Thus the first essential feature of the retina is that it amplifies the photon signal and converts it into macroscopic electric currents. ―Georgiev
The brain is thought to run more or less on direct current. This carries less information than light. For confirmation of this, look at the
byte transfer rate of fiber-optic cables vs electrical cables. Fiber optic signals can be modulated in many different ways. A channel can be modulated by frequency, by amplitude, by time, and by orbital angular momentum (not to be confused with the quantum mechanical term). These can be multiplexed onto the same waveform to carry far more information than a similar-sized DC wire at lower energy and higher speed.
Up to this point we have explicitly formulated the two most important points (facts) about visual perception that should be kept in mind by any researcher: namely there is (1) amplification and (2) irreversible processing of the visual information in the retina. ―Georgiev
He has done no experiment. His refutation of Hameroff up to this point is simply based on a textbook
Rube Goldberg Hypothesis of Photoconducion, a motley chimera created from the serial addition of ad hoc explanations.
Modern digital computers are based on digital electronic circuits within which the signals interact at gates that perform specific Boolean functions. All Boolean functions could be formed by various combinations of 3 elementary functions: AND, OR and NOT. These functions could be best appreciated by building a truth-table that illustrates all of the input-output relationships of a gate (cf. Mendelson, 1970; Kingsley, 1996). ―Georgiev
He admits that information is sent down the optic nerve, but he seems to think this is in the form of DC binary pulses and draws-upon prior articles with computer analogies. Still no mention of what structure within the axons themselves are responsible for carrying this current. Microtubules are the only continuous parallel structures within nerves, which are surrounded by non-conductive myelin. Szent-Györgyi (see above) and others proved that the conduction of direct current through a standard peptide backbone encounters a fairly high resistance, similar to rubber, with an experimentally-determined resistivity on the order of giga-ohm·meters. The photonic conduction of microtubules is yet to be determined, but experiments have confirmed that they do normally emit light. The lumen of microtubules are not opaque to the same extent that their backbones are resistive.
The last proposal of “quantum” visual perception to be discussed is proposed by Tuszynski’s group (cf. Salari et al., 2008; Rahnama et al., 2009) and involves quantum teleportation of photons. The authors propose that the visual photons are quantum teleported to the brain cortex and they collapse in the cortex instead inside the retina. ―Georgiev
Tuszynski's articles would then seem on par with Massimo Cocchi's . . .
The input of visual information to the brain cortex is a multistage process, in which the initial stimulus is registered by photoreceptor cells, converted into electric currents that affect the membrane potential and subsequently into altered release of neuromediator (glutamate) through exocytosis. The bipolar, horizontal and amacrine cells process the obtained information using graded potentials, while the ganglion cells and the neurons from LGN process the converted into action potentials information using a kind of Boolean binary logic. ―Georgiev
. . . and perhaps even Georgiev's himself.

These computer–brain analogies are about as old as computers themselves. Ray Peat talks about a entertaining instance of his:
In 1970, it was being seriously proposed that memory was produced by the death of brain cells, in a manner analogous to the holes punched in cards to enter data into computers. The cultural dogma made it impossible to consider that learning could be associated with the birth of new cells in the adult brain. ―Ray Peat*
And I don't see how vision could be pixelated. Is there any instance of a drug, vitamin deficiency, or brain injury causing one to see courser squares? All of the psychedelic indoles that I've had cause hallucinations based on smooth and colorful shapes. Consciousness is probably better modeled as complex waveforms, and vision can be seen as light flowing into the brain uninterrupted through microtubules inside the optic nerve.

I think Hameroff is fundamentally-correct in most ways, I'm just uncertain of the physical reality of quantum entanglement. I have to thank @Meatbag above for introducing me to Miles Mathis, who shines some light on this.

*Peat, Ray. "Stem cells, cell culture, and culture: Issues in regeneration"
 
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Travis

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Just learned from Miles Mathis a few interesting things. As it turns out, Karl Popper delivered a crushing blow to the Copenhagen School by publishing a powerful 38-page logical critique.
It was pretty good, but his explanation for the double-slit experiment wasn't. He lifted an explanation from a textbook by Alfred Landé that doesn't really seem to explain it—the same explanation used by Mathis.

Could the effect simply be that only certain angles are refracted off of the inner slit, or repelled by the subtle electrical charge of the metal grid? This is a good article to look at.

The diffraction pattern doesn't "disappear" when you only use one slit. You have to see a panoramic image to notice this, but the effect is there. Even a single-slit produces diffraction patterns.

(But the article below is hard to explain.)

 

meatbag

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Just learned from Miles Mathis a few interesting things. As it turns out, Karl Popper delivered a crushing blow to the Copenhagen School by publishing a powerful 38-page logical critique.
It was pretty good, but his explanation for the double-slit experiment wasn't. He lifted an explanation from a textbook by Alfred Landé that doesn't really seem to explain it—the same explanation used by Mathis.

Could the effect simply be that only certain angles are refracted off of the inner slit, or repelled by the subtle electrical charge of the metal grid? This is a good article to look at.

The diffraction pattern doesn't "disappear" when you only use one slit. You have to see a panoramic image to notice this, but the effect is there. Even a single-slit produces diffraction patterns.

(But the article below is hard to explain.)


I just skimmed Popper's paper and I don't think his explanation is the same since he never used the charge field emitted by the material which contains the slit through which the particle passes or assigned the same particle mechanics, or even mass, to photons as Mathis. Like Mathis says, every atom of the material is emitting particles called' Charge photons' that make up the charge field and interact with the observed photon particle by changing its spin property, deflecting, and changing its energy; and this creates the diffraction.

Here is a really good article by him on photon diffraction and the image it produces;
Rainbows, Prisms, and non-edge Diffraction by Miles Mathis

How do photons travel?;How do photons travel by Miles Mathis

Photon mass and how it relates to the Electron; Unifiying the photon by Miles Mathis
And his article on the Double slit experiment specifically; The Double Slit Experiment by Miles Williams Mathis
 
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noordinary

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Is it me or this tread starts to sound like porn? lol
Thank you guys, i know what i'll be reading Saturday morning!
 
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Travis

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I just skimmed Popper's paper and I don't think his explanation is the same since he never used the charge field emitted by the material which contains the slit through which the particle passes or assigned the same particle mechanics, or even mass, to photons as Mathis. Like Mathis says, every atom of the material is emitting particles called' messenger photons' that make up the charge field and interact with the observed photon particle by changing its spin property, deflecting, and changing its energy; and this creates the diffraction.
You're right. Mathis' double-slit article was the first one that I had read. I then went on a reading spree where I had read a few more Mathis articles and then found the Popper article. I didn't like Mathis' use of the messenger photons, wiped-it from my short-term memory, and later confounded his many other Popper affirmations and references contained in this article with his adherence to Popper's—or should I say Landé's—brief explanation of the double-slit effect.

If you look at the second article, you can see what appears to be a diffraction pattern in a single-slit setup. I should look for more examples of this. I agree with Mathis in that the metal if the slit is causing the diffraction (it's better than Popper's) but think it could be more easily explained by just the metal's electrons and perhaps, dare I say, surface plasmon polaritons—something certainly Bohr nor Popper could possible have known about back then.

This article is a non-Sci-Hub article and is the most popular article on surface plasmon polaritons. It's been cited 9197 times.

But the effect is actually fairly well-understood by some, and long textbooks have been written on it. Surface polaritons are waves which travel along the surface of metals which can be best illustrated by an electric field intensity distribution . . .(Fukuhara, 2014)

polariton.png
click to embiggen


. . . and mathematically-modeled using both equations from optics and electrodynamics, the two areas of interest. Instead of inventing a new virtual photon like Mathis, perhaps it could be explained with concepts already well-established?

Polaritons are used primarily in the telecommunications industry, as optical–copper interfaces sit at the junction between high-speed fiber-optic cables and modems. There are ways to turn optical signals into DC pulses without semiconductors.

Also of interest is that the wavelength of the surface plasma polariton—a chimeric light and metal fusion wave so inexplicable that they were forced to invent a term equally bizarre to describe it—is actually greatly reduced when it fuses with the metal. This reduction in wavelength is seen as doubleplusgood by physicists, who see it as yet another step towards miniaturization (dimutation). Whether light couples with the metal surface or reflects depends greatly on the incident angle, and it's probably not a stretch to think that the wide panaramic diffraction fringes seen in the single-slit experiment could perhaps have been created by a surface plasmon polariton getting trapped (coupled) on the metal grid's edge, rounding to corner at reduced wavelength, and then being emitted at a shallower angle more perpendicular to the original light path.

The image below is from light passing through one slit only (Bach, 2013):

single slit.png click to embiggen

And there is also the older photoelectric and Compton effects which may have some relevance. Some light must be reflected off each slit's outer edge towards the centre.

I think the diffraction pattern seen with two slits could merely be a non-interacting superposition of the two individual patterns, one from each slit. Much of the confusion comes from the points that Karl Popper outlines, and also from the simple fact that the wave interference pattern of two slits is commonly modeled as if they were ocean or sound waves (see: just about any diagram)—these are pressure waves. Seen in this way, it does seem quite impossible that firing photons one-by-one would produce interference.

. . . and that myth that a single slit does not show diffraction.
 
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meatbag

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a new virtual photon like Mathis,

It is NOT a virtual photon, it is a real mass photon. I should not of used the term ' messenger photon' , absolute rookie error :/ and I apologize to all involved... Mathis' particle is the 'Charge Photon', totally different things.

The characteristics of the charge photon are described in this paper; http://milesmathis.com/photon3.pdf

Surface polaritons are waves which travel along the surface of metals which can be best illustrated by an electric field intensity distribution

And how exactly are these waves interacting with the photons to create the diffraction pattern?
 
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Travis

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And how exactly are these waves interacting with the photons to create the diffraction pattern?
Those waves actually are the photons, after they have been captured by the metal surface. They then can be emitted later at a lower frequency. The angle of incidence determines whether or not a photon is captured and guided along a metal surface. If you wan't to know how they behave around two slits, you could perhaps read these articles:

The idea was that there are at least four ways that light interacts with metal: By reflection, Compton Effect, Photoelectric Effect, and by becoming surface plasmon polaritons. So nobody should be troubled by the fact that shooting electrons one-by-one also creates regular diffraction patterns. The simple answer might be that the light is reflected, repelled, absorbed–emitted, and absorbed–travelled–emitted by the slit's edge and inner surface.

I think it only seems bizarre when you originally imagine light waves as ocean or sound waves. Below is Richard Feynman making water analogies, referring to the mask as "barges" lined-up with gaps and the electron detector as "buoys." This is setting-up the audience for later "gotcha" moments,



. . . in which the viewer is is left astonished. This only happens because they were given given exaggerated drawings and forced to accept water-wave analogies. Like a magician Richard Feynman delivers mind-blowing conclusions one after another which logically follow from the ocean wave analogy and Heisenberg's so-called "Laws," and delivers the prestige a bit after the 50 minute mark.
I was like: Whooa! Mind-blown, Seth. ―Cecily Strong
University deans probably like it since it makes physics sound fun and mystical . . .They're not just science hacks anymore, they are brilliant philosopher–artists who have serendipitously discovered the most profound secrets of life simply from shining light through two slits. Join Calctech Physics Department: Be the shaman of science.
Feynman was fond of saying that all of quantum mechanics can be gleaned from carefully thinking through the implications of this single experiment. ―Wikipedia
I'll have to take a look at Mathis' article on photons. I found the one on
π to be especially good. It was shocking and I'm fairly certain he's 100% correct. I think you could could say that he had effectively proved it.
 
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Travis

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And destructive interference from crossing light "waves" (beams) appears to by a myth. I have seen dozens of photos of laser beams crossing paths and not one shows an instance of destructive interference. No darkening; no wavelength shifts; no changes in color; just the simple addition of amplitudes (intensity). It would be ridiculous to assume that the "interfering" beams had been perfectly in phase in every instance, a near statistical impossibility.

Treating light rays as oscillating sine waves might then seem about as appropriate as modeling them as pressure waves propagating through a medium.
 
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schultz

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linseed oil really is bad-tasting.

Someone needs to tell the chickens this

Haha, yah I am not fond of the taste myself. A while back I was talking to the local feed store operator about the different chicken feeds they have. The most expensive feed they have is the one they use for "omega-3 eggs". It has added vitamins and stuff, but also flax seed. It's not a pellet but different loose grains and he said it might not be worth getting because the chickens tend not to eat the flaxseeds and they are left at the bottom of the feed container when all the rest of the grains have been consumed. So I am not even sure chickens like flax seeds lol.

Linseed oil is used in a lot of things, besides paints. Window putty, the putty they put on old windows to install the glazing, is made with linseed oil and it becomes quite hard. Another product made with linseed oil is true linoleum (not vinyl) where it is mixed with cork. Yes it is good for making floors lol. Traditionally the oil is boiled which helps kickstart the polymerization process. Other ways they "boil" linseed oil are by blowing oxygen through it or by adding heavy metals to the oil. Now ponder that for a bit while thinking about what lipofuscin is. Similar processes are happening inside the body. Lipofuscin is synonymous with aging.

Something else that's interesting is that a rag that has been used to wipe boiled linseed oil will spontaneously combust if left out because of the polymerization. That's how quickly the reaction happens. Yes, really, rags will burst into flames.



Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells. - PubMed - NCBI
"In experimental model systems, lipofuscin accumulation can be accelerated by increased oxidative stress and by inhibition of lysosomal proteases and lipases, conditions that promote the aging process in general. Consequently, the accumulation of lipofuscin is regarded as one of the best-known markers of aging."

Specific lipofuscin staining as a novel biomarker to detect replicative and stress-induced senescence. A method applicable in cryo-preserved and archival tissues
"Lipofuscin is a non degradable aggregate of oxidized proteins, lipids and metals which accumulates inside the lysosomes of cells that do not replicate."

The question is, does lipofuscin accumulate in cells that have already stopped replicating or does lipofuscin itself cause the cell to not be able to replicate and/or repair itself? I suspect the latter.

Here is a quote from the first paper I posted:

"So it was demonstrated that lipofuscin is able to inhibit the proteasome, the most important cellular system for proteolytic degradation of damaged, modified, or misfolded proteins."
 

meatbag

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Those waves actually are the photons, after they have been captured by the metal surface. They then can be emitted later at a lower frequency. The angle of incidence determines whether or not a photon is captured and guided along a metal surface. If you wan't to know how they behave around two slits, you could perhaps read these articles:
The idea was that there are at least four ways that light interacts with metal: By reflection, Compton Effect, Photoelectric Effect, and by becoming surface plasmon polaritons. So nobody should be troubled by the fact that shooting electrons one-by-one also creates regular diffraction patterns. The simple answer might be that the light is reflected, repelled, absorbed–emitted, and absorbed–travelled–emitted by the slit's edge and inner surface.

I think it only seems bizarre when you originally imagine light waves as ocean or sound waves. Below is Richard Feynman making water analogies, referring to the mask as "barges" lined-up with gaps and the electron detector as "buoys." This is setting-up the audience for later "gotcha" moments,



. . . in which the viewer is is left astonished. This only happens because they were given given exaggerated drawings and forced to accept water-wave analogies. Like a magician Richard Feynman delivers mind-blowing conclusions one after another which logically follow from the ocean wave analogy and Heisenberg's so-called "Laws," and delivers the prestige a bit after the 50 minute mark.

University deans probably like it since it makes physics sound fun and mystical . . .They're not just science hacks anymore, they are brilliant philosopher–artists who have serendipitously discovered the most profound secrets of life simply from shining light through two slits. Join Calctech Physics Department: Be the shaman of science.

I'll have to take a look at Mathis' article on photons. I found the one on
π to be especially good. It was shocking and I'm fairly certain he's 100% correct. I think you could could say that he had effectively proved it.


I think the idea is based on the Drude-Sommerfeld model which Mathis' also has an article abut;http://milesmathis.com/drude.pdf

I remember being shown some excerpts of that, I'll have to watch the whole thing.

Also if your on Mathis' site be sure to check out his beautiful paintings, they're amazing :singing:
 
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Travis

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@schultz — That second link was interesting. They found that when staining lipofuscin directly, it co-localized with β-galactosidase. This is a purported enzyme that is "found only in senescent cells." Even Wikipedia admits that it's a hypothetical enzyme–noun:
Senescence-associated beta-galactosidase (SA-β-gal or SABG) is a hypothetical hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides only in senescent cells. Senescence-associated beta-galactosidase, along with p16, is regarded to be a biomarker of cellular senescence. —Wiki
But it's discoverer speaks as if were real:
We show that several human cells express a β-galactosidase, histochemically detectable at pH 6, upon senescence in culture. [...] Senescent human fibroblasts expressed a β-Gal that was detected in single cells by X-Gal, which forms a local blue precipitate upon cleavage (24), independent of DNA synthesis measurements. [...] Cells from all three embryonic layers expressed β-Gal upon senescence in culture.† —Dimri
But the discoverer also refers to the enzyme as a verb, as well as a hypothetical noun.
Early passage adult melanocytes grew well in culture, yet >90% expressed pH 6 β-Gal activity. —Dimri
Enzymes are often named before they are even isolated, based on their activity alone. They are sometimes known as enzyme–verbs before they are enzyme–nouns. But even speaking about every chemical reaction as enzymatic seems premature in many cases, as many chemical reactions happen nonenzymatically.

  • Keller, Markus A., Gabriel Piedrafita, and Markus Ralser. "The widespread role of non-enzymatic reactions in cellular metabolism." Current opinion in biotechnology 34 (2015): 153-161.
A plausible primordial base can be traced for glycolysis and the PPP, as several of their reactions can be replicated with metal catalysts, in particular Fe(II), under conditions reproducing the ocean chemistry of the Archean world [8]. Fe(II) was broadly available before oxygenation of the early Earth [9], implying a scenario for the first glycolytic enzymes being simple iron-binding RNA or oligopeptide molecules, which would have possessed the potential of enhancing many reactions now found in central metabolism [7,8] (Box 1). —Keller
But it seems to be the fashion among biologists to ascribe every single chemical reaction to an enzyme, even one which can happen spontaneously. Every phosphorylation, acetylation, hydroxylation, dehydrogenation, and . . . even reductions. This leads to extremely complex reaction cascades, in which areas of phosphorylation are so impossibly crowded by diverse apparitions of kinases and phosphodiesterases that it makes you wonder how space can be made available for everyone's hypothesized mechanism. But everyone must have their glory, right? Everyone wants to name a molecule or pathway, to stake their name on it like like Buzz Aldrin impaling a flagpole on the Moon.

Ray Peat said once wrote that the amount of receptors presumed to exist on the cell membrane actually exceeds the surface area of said membrane. I predict that new unicorns will continue to be manufactured until the point is reached where the virtual cell has a virtual density of 2 g/ml.

The fact that β-galactosidase activity at pH 6 had been discovered to be lysosomal in nature (Lee, 2006), and that it later had been found to co-localize with lipofuscin (Georgakopoulou, 2013), leads me think that β-galactosidase activity at pH 6 is from the lipofuscin itself: From the iron.

Here is the fluorescent stain used to detect β-galactosidase activity, in senescent cells, at pH 6.

indol-1.png

Tentatively-hypothetical β-galactosidase cleaves at the C–O–C ether bond, but Iron has been shown to do this nonenzymatically:

Here, we report iron-catalyzed deallylations that selectively cleave functionalized ethers under mild conditions . . . ―Gärtner

Mild conditions indeed. Iron chloride in xylene cleaved the ether bond in high yield. The one most similar to the "β-galactosidase" substrate is number 7 (bottom left). The yield was 92%.

iron ether2.png


And according to Dr. Richard Zepp,‡ the rate of of the iron-catalyzed Fenton reaction increases with decreasing pH, through the range of pH 8⟶5. This would explain why the assay is only selective to senescent cells when carried-out at pH 6.

I think you're almost forced to conclude that β-galactosidase activity, or the cleavage of β-galactosidic bonds, is simply the result of the Fenton reaction. It would then not be an enzyme activity at all, but a catalytic activity. β-galactosidase would then technically be a catalyst, not an enzyme, and it would be the lipofuscin itself: Iron atoms immobilized on the matrix of polymerized lipid peroxidation products; dialdehydes Shiff-linked to polyamines and/or protein-based –N₃⁺, such as those of lysine and arginine. Either it's the iron doing this, or you're forced to believe that the body creates a special enzyme only for the lysosomes of old people which only works at the unphysiological pH of 6.
@schultz ― Another product made with linseed oil is true linoleum (not vinyl) where it is mixed with cork. Yes it is good for making floors lol.
Yeah. I always correct people on that. You could have noticed my penchant for not using genericizing trade names, even to the point of saying such things and "transparent tape" if it happens to be from 3M® and not Scotch®. Here is a list of quite a few generic trade names which have invaded the lexicon like a clown who had snook under the tent flap, or . . . like linoleic acid being force-injected into reconstituted cork tile.
Traditionally the oil is boiled which helps kickstart he polymerization process. Other ways they "boil" linseed oil are by blowing oxygen through it or by adding heavy metals to the oil. Now ponder that for a bit while thinking about what lipofuscin is. Similar processes are happening inside the body. Lipofuscin is synonymous with aging.
I went read a few lipofuscin articles a few months ago. The best ones, in my opinion, are from Terman and Brunk. Here is a full-text link to one of the review articles.

Artists have noticed this. Some oil paint colors dry faster than others; some metal pigments increasing the "drying" rate of the oil. Windsor & Newton have kindly tabulated the drying time of their oils. You will notice that the faster drying colors are the ones with transition metal pigments, and the slower ones are the metal-free polycyclic fluorophores such as alizarin crimson. Iron tops the list, but iron is not explicitly named (hint: iron oxide is found in burnt sienna).
The question is, does lipofuscin accumulate in cells that have already stopped replicating or does lipofuscin itself cause the cell to not be able to replicate and/or repair itself? I suspect the latter.
From what I remember Brunk and Terman saying: Lipofuscin accumulates mainly in non-renewing cells. The first time that I had become aware of such non-mitotic cells was from them. Some cells always divide and dilute the lipofuscin, but some cells do not. Some cells of the central nervous system accumulate the most lipofuscin since they don't have the benefit of dividing at a high rate.

*Lee, Bo Yun, et al. "Senescence‐associated β‐galactosidase is lysosomal β‐galactosidase." Aging cell 5.2 (2006): 187-195.
†Dimri, Goberdhan P., et al. "A biomarker that identifies senescent human cells in culture and in aging skin in vivo." Proceedings of the National Academy of Sciences 92.20 (1995): 9363-9367.
‡Zepp, Richard G., Bruce C. Faust, and Juerg Hoigne. "Hydroxyl radical formation in aqueous reactions (pH 3-8) of iron (II) with hydrogen peroxide: the photo-Fenton reaction." Environmental Science & Technology 26.2 (1992): 313-319.

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Perhaps of interest is the action of prolactin on the cell. This hormone powerfully increase the intracellular calcium concentration. It can do this in single-digit nanomolar concentrations. It's stunning, really. I just got done reading about this yesterday. Here is a series of photographs taken every 400 milliseconds (their shutter speed was actually quicker than this, but they only posted every ten frames.)

prolactin5.png click to embiggen

A calcium wave is initiated upon prolactin binding. The flourophore chelates calcium and and this shifts it peak frequency of fluorescence from ~480nm to ~400nm. The fluorophore itself (left) is interesting; it has two γ-carboxyglutamate-like domains (right).

fluoro.png click to embiggen

Which must be the calcium-chelating domain. Vitamin K helps to turn glutamate residues of proteins to γ-carboxyglutamate (right). The proteins are then able to chelate calcium with this modified, double-carboxylated glutamate. Bone forming proteins such as osteocalcin have calcium-chlating γ-carboxyglutamate domains, which are almost certainly the areas where the small hydroxyapatite crystals initially form and nucleate on bones. The rest of the bone is basically collagen and has no particular affinity for calcium.

A lack of vitamin K, or the ingestion of Warfarin®, can lead to calcium precipitating out of the blood and calcifying arteries—even to the point of giving them a chalk-like appearance.

You might thing that calcium²⁺ binding strongly to the dicarboxy²⁻ group would draw electrons away from the ring, towards the nitrogen. This change in polarity, or Ling's c-effect, is likely what causes the shift in fluorescence. Resonate rings with double-bonds have delocalized π-electrons which travel freely everywhere in the ring. This is why graphite is so much more electrically-conductive that diamond—both carbon.
 
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Amazoniac

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Artists have noticed this. Some oil paint colors dry faster than others; some metal pigments increasing the "drying" rate of the oil. Windsor & Newton have kindly tabulated the drying time of their oils. You will notice that the faster drying colors are the ones with transition metal pigments, and the slower ones are the metal-free polycyclic fluorophores such as alizarin crimson. Iron tops the list, but iron is not explicitly named (hint: iron oxide is found in burnt sienna).
What about the iron oxide in sunscreens to change the white of the zinc oxide to the tone of the skin?
 
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Travis

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What about the iron oxide in sunscreens to change the white of the zinc oxide to the tone of the skin?
I don't like the idea, and this is the first time that I heard about such a thing.
 
EMF Mitigation - Flush Niacin - Big 5 Minerals

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