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Dr. Martin Pall EMF interview from Electric Sense - awesome!

Discussion in 'The Cave' started by Penny, May 17, 2014.

  1. Penny

    Penny New Member

  2. Jack Kruse

    Jack Kruse Administrator

    This guy is a horrible listen......The guy who asked about electrons and chi force was hitting on the key and Pall flubbed it badly........He also knows nothing about Becker's work. Really really terrible in my view. He also can not link the calcium channels to the 3 legged stool or why the NO and ONOO pathway links to cardolipin c in mitochondria in cytochrome 4.
     
  3. Jack Kruse

    Jack Kruse Administrator

    I think it is hilarious he says at the end the seafood diet is the way to go because of NRF 2. My book is all about that.

    But the next book is about how the entire process is quantized.........

    Maybe I'll give you a preview of the next book
     
    Last edited: May 18, 2014
  4. Josh

    Josh Gold

    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2965188/

    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2932530/

     
  5. Josh

    Josh Gold


    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732771/figure/F6/

     
  6. Jack Kruse

    Jack Kruse Administrator

    The enzyme cytochrome c oxidase or Complex IV, is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes.

    It is the last enzyme in the respiratory electron transport chain of mitochondria (or bacteria) located in the mitochondrial (or bacterial) membrane. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. In the process, it binds four protons from the inner aqueous phase to make water, and in addition translocates four protons across the membrane, helping to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP which withdraws electrons to unfold proteins and allows them to unfold fully for maximum water binding.

    The complex is a large integral membrane protein composed of several transition metal prosthetic sites and 14 protein subunits in mammals. In mammals, eleven subunits are nuclear in origin, and three are synthesized in the mitochondria themselves. The complex contains two hemes, acytochrome a and cytochrome a3, and two copper centers, the CuA and CuB centers (think OSF 3 where I said transition metals wont be too far from the movement of electrons).
    In fact, the cytochrome a3 and CuB form a binuclear center that is the site of oxygen reduction. Cytochrome c, which is reduced by the preceding component of the respiratory chain (cytochrome bc1 complex, complex III), docks near the CuA binuclear center and passes an electron to it, being oxidized back to cytochrome c containing Fe3+. This action all happens because of the D shell electrons in these transition metals. They are easily translocalized because of the relationship of the atomic mass to electron cloud. The reduced CuA binuclear center now passes an electron on to cytochrome a, which in turn passes an electron on to the cytochrome a3-CuB binuclear center. The two metal ions in this binuclear center are only 4.5 Å apart and coordinate ahydroxide ion in the fully oxidized state. Why is this big? Anything over 8 Angstroms can no longer quantum tunnel electrons in the between the cytochromes.

    DPA is over 8 Angstroms.........DHA is just a shade over 6 Angstroms. This is why Lady evolution selected DHA to capture electrons in your brain and all cell membranes
     
  7. Jack Kruse

    Jack Kruse Administrator

    X ray Crystallographic studies of cytochrome c oxidase show an unusual quantum post-translational modification, linking C6 of Tyr(244) and the ε-N of His(240) (bovine enzyme numbering). This means the relationship is not coded for in your DNA, but with proper protein construction the relationship is maintained without having to be made. This is another example of the quantum mechanism at play from OSF 3.

    This is how a zero entropy machine self assembles using quantum laws.............

    This unusual relationship in cytochrome c plays THE vital role in enabling the cytochrome a3- CuB binuclear center to accept four electrons in reducing molecular oxygen to water.

    So if the relationship is not maintained...........by the electromagnetic force what happens?

    You lose electrons tunneling.

    One or two we have the answer for.........SOD 1 can handle that...........greater than two and we get Fenton reactions which firther destroy this tight quantum couple..........

    What happens? More space leads to more calcium influx = higher nitric oxide.........= more lipid peroxidation =
    increase peroxynitrite (abbreviated PRN) which can stimulate oxidative stress which can stimulate NF-kappa B and IL 6 (Think CPC 8 or the early leptin series blogs) which can increase the production of iNOS which can, in turn increase nitric oxide even further. This loop becomes a death spiral because calcium activates voltage gated and NMDA channels to swell the mitochondria to liberate cytochrome c. This mechanism alone constitutes a potential vicious cycle and there are a number of other loops that tie into the NRF 2 pathways............which all lead to p53= protector of the genome = cancer.

    The mechanism of reduction linking C6 of Tyr(244) and the ε-N of His(240) was formerly thought to involve a peroxide intermediate, which was believed to lead to superoxide production. But new data says this is not the case. The reason we do not know is because the real chemistry is 100% linked to the environment's redox state and it always varies making measurements near impossible. This shows you the magic of OSF 3 yet again.

    The currently accepted mechanism involves a rapid four-electron reduction involving immediate oxygen-oxygen bond cleavage, avoiding any intermediate likely to form superoxide. When this couple breaks..........all hell breaks lose.

    This is where non native EMF acts directly in your mitochondria.

    BOOM
     
    Martin and Josh like this.
  8. Jack Kruse

    Jack Kruse Administrator

    Now for more quantum magic? Where is the cytochrome c that controls your change programs in mitochondria located? Where is it assembled and do you think this matters in mass equivalence?

    If you got T2 D you better pay close attention.

    The site of assembly of cytochrome c is believed to occur near TOM/TIM. TOM/TIM I spoke about in the first 4 blogs I ever wrote about in the mitochondrial series I abandoned because of the complexity. It has taken me close to 4 yrs to scale you back to it. That is how slow I have gone. LOL

    The TIM/TOM complex is a process in cellular biochemistry which describes the translocation of proteins produced from nuclear DNA through the mitochondrial membrane for use in oxidative phosphorylation. Only 13 proteins necessary for a mitochondrion are actually coded in mitochondrial DNA. Just 13....................but man are they key. (EE 12)



    TOM = Mitochondrial membrane transport proteins. They are small chaperone proteins which exist in the membranes of mitochondria and which serve to transport molecules and other factors such as ions into or out of the organelles. Can anyone say so here is where calcium destroys us?

    The TIM/TOM complex joins nuclear and mitochondrial intermediates and makes them self assemble and allows them to be accessible to bind with subunits imported from cytosol. This construction is 100% quantized!!!! Surprise!
    And when the right amount of quanta is not present guess what happens at TIM/TOM?

    You get T2D or metabolic syndrome.

    BOOM

    Heme ions (transition metal alert) and cofactors are inserted into subunits I & II by this complex. Subunits I and IV initiate quantum assembly. Other subunits may form sub-complex intermediates that later bind to others to form COX complex. COX complex = cytochrome c oxidase.
    Cytochrome c oxidase (COX) deficiency causes a variety of neuromuscular and non-neuromuscular disorders in childhood and adulthood and can theoretically undergo either a nuclear or a mitochondrial (mt) mode of inheritance, making genetic counseling in COX deficiency particularly hazardous. These are all maternal inherited conditions. Darwin had one of them ironically and why he always felt better dumping cold water on himself........because it lowered his mass to offset his swollen mitochondria!!!!

    BOOM


    In post-assembly modifications, the enzyme is dimerized, which is required for active/efficient enzyme action. Dimers are connected by a cardiolipin molecule. Now think Jeremy? What anchored him? His CFTR defect.........and it cant in CF. Cardiolipin does the same thing your mitochondrial membranes.

    If you have anti-phospholipid syndrome what can't you do well? Bind cardiolipin. Seeing some scaled homology yet? OSF 3 is everywhere you look.........once you understand it.
     
  9. Jack Kruse

    Jack Kruse Administrator

    So how do you get T2D?

    Bad quantum construction of the cytochromes at the COX complex

    The vast majority of proteins destined for the mitochondria are encoded in the nucleus and synthesized in the cytoplasm of our cells.

    These are tagged by an N-terminal signal sequence. Funny thing...........did you know prion activation occurs the same way? Bread crumb from OSF 3 mechanism!

    Following transport through the cytosol from the nucleus, the signal sequence is recognized by a receptor protein (another OSF 3 example) in the transporter outer membrane (TOM) complex. The signal sequence and adjacent portions of the polypeptide chain are inserted in the TOM complex, then begin interaction with a transporter inner membrane (TIM) complex based upon the REDOX state. When you are oxidized, (think T2D or any disease really) you can not optimally build you cytochromes to tunnel electrons. You think this is good news for your mitochondrial change programs that control its size and shape?

    What does size and shape do to mass equivalence........?? BOOM


    When the redox is good all is well........when it sucks, like most here have we get problems in quantum construction. The polypepetide chains do not assemble and fold correctly (OSF 3 alert yet again) This action has to be perfectly quantized so linkage and protein folding can occur at sites of close contact between the two membranes in mitochondria. The protein signal sequence is then translocated into the matrix of the mitochondria in a process that requires an electrochemical hydrogen ion gradient across the inner membrane. This is why water charge separation is huge. What makes this hydrogen gradient? When water is next to a hydrophilic cell memebrane what did Pollack say happens without any energy?

    We make an EZ that has a huge hydronium ion layer of protons? What is a proton? It is a hydrogen ion. BOOM

    Told ya I had it down. Took long time to get here.
     
    Martin likes this.
  10. Jack Kruse

    Jack Kruse Administrator

    REmember the quantum mechanism in OSF 3...........quanta alters proteins energy profile to directly alter their physiology abilities?

    Now consider as the cytochrome proteins are moving through the two membranes and the mitochondria via compartments..........what controls the final confirmation?

    I'll give you a hint.........It is not Darwin or Dawkins RNA or DNA!!!

    It is another chaperone protein.

    See this OSF 3 mechanism is everywhere.................

    Mitochondrial Hsp70 binds to regions of the polypeptide chain and maintains it in an unfolded state as it moves into the matrix.

    Just for kicks..........did you know that heat chock proteins (Hsp70) have their own levee in the QUILT too?

    BOOM

    CITE:

    B. Alberts, A. Johnson, J. lewis, M. Raff,. K. Roberts, P. Walter. Molecular Biology of the Cell
     
  11. Jack Kruse

    Jack Kruse Administrator

    Chaperone proteins have something in common...........length and shape are always tied to quanta added or subtracted. They are small proteins made up of alpha and beta sheets.

    The redox potential determines how much of each one is present. The percentage then determine physiologic function.

    This is how prion diseases occur. OSF 3 is everywhere.

    Did you know the two chaperone proteins for RNA and DNA are called methylation and acetylation proteins..........

    Guess how they work?

    BOOM
     
  12. Jack Kruse

    Jack Kruse Administrator

    The Hsp70s is 70 kilodaltons. Daltons are a way we can measure a proteins mass.

    Surprise!!!

    I told you DHA has been king of mammalian evolution and has dictated to DNA for 600 million yrs.

    HSP 70 has a better record than DHA. It has been conserved ubiquitously in all life.


    Think it might be important?




     
  13. Jack Kruse

    Jack Kruse Administrator

    The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress!!!


    OSF 3 shows up yet again.


    So how does HSP70 act?

    Depends upon the quanta of energy added or subtracted to determine what it can and cant do and where it can or can not act.
     
  14. Jack Kruse

    Jack Kruse Administrator

    You know that whole mammal thing about making our own heat and how that IR heat Pollack found we can use to charge separate water without light present?

    Members of the Hsp70 family are strongly upregulated by heat stress and toxic chemicals, particularly by heavy metals and transition metals such as arsenic, cadmium, copper, mercury.

    BOOM


    I hope y'all are feeling this all................lots of fireworks need to be going off about now.

    I have built a lot of foundational knowledge that you must begin to use and assimilate to innovate your N =1
     
  15. Jack Kruse

    Jack Kruse Administrator

    The Hsp70 proteins have three major functional protein domains:

    • N-terminal ATPase domain – binds ATP (Adenosine triphosphate) and hydrolyzes it to ADP (Adenosine diphosphate). The exchange of ATP drives conformational changes in the other two domains. Hsp70 is usually in the ATP confirmation. What does this do to Hsp70? ATP withdraws electrons from it to give it to another protein where it is attracted to by vander wall forces, electrostatic attraction, hydrogen bonding which are controlled by what? The electromagnetic force the cell senses.

    • Substrate binding domain – contains a groove with an affinity for neutral, hydrophobic amino acid residues. The groove is long enough to interact with peptides up to seven residues in length. So when water is not around a protein for any reason here is where Hsp70 bonds to give up its quanta of energy to limit the shape and size change. If you heat up a chromosome Hsp70 allow the places without water micelles around them to form balls on the nucleic acid to protect it.

    • C-terminal domain – rich in alpha helical structure acts as a 'lid' for the substrate binding domain. What did I say above about alpha helical shape? It shows up when electrons are plentiful and when protons are not. When protons are plentiful we see beta shape phase transition.

    • When an Hsp70 protein is ATP bound, the lid is open and peptides bind and release relatively rapidly to transfer quanta of energy. When Hsp70 proteins are ADP bound, the lid is closed, and peptides are tightly bound to the substrate binding domain.
    ALL tied to electrons..................
     
  16. Jack Kruse

    Jack Kruse Administrator

    Hsp70 are the back up system to make ATP faster when water is not around.............

    This protein is Ben Greenfield, Dave Asprey, and Robb Wolf's only saving grace that what they do and advocate do not explode their PPP to replenish NADPH to make ATP the old fashion way we humans should.
     
  17. Jack Kruse

    Jack Kruse Administrator

    When proteins are being assaulted for any reason Hsp70 is the crew that comes in and tries to maintain TENSEGRITY in the cell

    Where have you heard that word before?

    LOL

    Hsp70 also aids in transmembrane transport of proteins, by stabilizing them in a partially folded state. A protein is in that state why? Cause it lost quanta of electrons and bending confirmation changes............

    This is how we go alpha to beta protein transition folks............

    Foundational quantum evolutionary change in proteins. OSF 3 yet again.
     
    labellavita likes this.
  18. Jack Kruse

    Jack Kruse Administrator

    Enough.........you can read the new book when I am done.............

    I got to get a glass of wine, and swim hypoxically now to lose some weight.

    Bread crumb alert.
     
    Josh likes this.
  19. prAna303

    prAna303 New Member

    Sounds like a freedive to me... Had myself some good times in the sea today, +6C in the water and +23C in the air, static training for an hour. I am diving into a good cognaq myself.
     
  20. Clayton

    Clayton New Member

    Kinda like listening to this guy..

     

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