1. Registering for the Forum

    We require a human profile pic upon registration on this forum.

    After registration is submitted, you will receive a confirmation email, which should contain a link to confirm your intent to register for the forum. At this point, you will not yet be registered on the forum.

    Our Support staff will manually approve your account within 24 hours, and you will get a notification. This is to prevent the many spam account signups which we receive on a daily basis.

    If you have any problems completing this registration, please email support@jackkruse.com and we will assist you.


Discussion in 'Educating Doctors' started by Jack Kruse, Jul 23, 2019.

  1. Jack Kruse

    Jack Kruse Administrator


    This post is loaded with so many anti-aging marketing meme’s it is sickening. Let take apart one, #7. I am a neurosurgeon so protein misfolding is an expertise of mine. Most people are unaware that we can monitor protein misfolding dynamics because of the hydrogen/deuterium exchange process. This can be done via mass spectrometry (HDX-MS). HDX-MS has emerged as a powerful method for characterizing protein conformational dynamics in cells. The basis of this method is the fact that backbone amides in stable hydrogen-bonded structures (e.g., α-helices and β-sheets) are protected against exchange with the aqueous solvent. All protein structures in humans are hydrated with some form of water with a varying amount of Hydrogen to deuterium mix based upon its location in the cell. All protein structures become dynamic because of this arrangement because of information protons bring or subtract from the proteins in question. These protons are created when light hits the hydrogen bonding network in water to exclude protons. This is how light acts as an information processor in cells. This even plays a massive role in DNA/RNA helices. It is also clear from these protein studies, however, that eventually all of the protecting hydrogen bonds will transiently breakdown as the protein — according to quantum thermodynamic principles — via cycles that control folding.

    The redox power (light) in the water surrounding proteins controls this process in protons. So if we change the fraction of H+/D around a protein we can see with mass spectrometry how protons impart information and energy to amino acids amine bonds by examining their partially unfolded states. These changes correspond to excited free energy and information levels. As a result, all of the backbone amides in biomolecules can and will eventually become temporarily solvent-exposed and exchange-competent over time as life is lived. The environment controls the fractionation of the surrounding water. This is how protein folding occurs in mast cell diseases and many other disorders of protein folding (AD, PD, ALS). Consequently, a folded protein in D2O will gradually incorporate deuterium into its backbone amides over H+, and the kinetics of the process can be readily monitored by mass spectrometry when we know where and what to look for. I expect this to be part of quantum medicine in the future. Nothing in this paper talks about this. This is a fluff marketing piece with science subtracted.

    Alex97232 and Ed Pomicter like this.
  2. Proteins either start folding as soon as they emerge from a ribosome as chains of amino-acid residues or require a helper molecule to fold into a well-defined three-dimensional structure, which is essential for their proper functioning. Misfolding is often a result of insufficient internal free energy.

    My question: From an electromagnetizm perspective, would it be therapeutic to increase the electrical charge in the extracellular plasma? If so, what would a DC pulsed frequency (say 7.83 Hz) and voltage (say at least negative 50 milliwatts), delivered through myelin sheath conduits (creating completed electric circuits) while administrating IR light, provide to the electron transport (charged ions) in the extracellular plasma? Would it become "super charged", enhancing the "free" ions' potential for a greater therapeutic effect?

    Most biological studies of proteins trek through the funnel of folding and unfolding only assume what occurred from point "A" to point "B" when analyzed under the organic-chemistry microscope. Specifically, how it is believed electrons (from helper molecules) might work (or move) from one chemical transformation to the next.

    I have read "Light Shaping Life" and I'm astonished how little we know! Nature has so much to teach us. Are we ready (trainable) for her lessons?
    JanSz likes this.

Share This Page