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Post by lilsissy on Nov 11, 2013 11:35:09 GMT -5
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Post by skyship on Nov 12, 2013 3:03:56 GMT -5
Lil Sis, So sorry to hear of your mother passing. It seems the "jinn" was present and everything came unglued. those dark spirits of ester....... and they wreck havoc in our lives. Yet, we know there is a higher, brighter spirit that can bring that "jinn" to its knees. May this spirit of love come back to your family. *********************************************** Yes, the alginate mixes with the sup35 nanowire. And this too can rearrange the cytoskeleton. ......." Major degenerative diseases of skin, muscle, and neurons are caused by disruption of the IF cytoskeleton or its connections to other cell structures."............. www.ncbi.nlm.nih.gov/books/NBK21560/#A5562====================== Here are the metal nanowires made from amyloid, specifically sup35: [[/b] Self-assembly of amyloidogenic peptides into fibril nanostructures can play an important role in building nanowires and nanoelectronic materials. For example, nanotubes made by the self-assembly of Phe-Phe dipeptide from the central region of amyloid β-peptide (Aβ, associated with Alzheimer's disease) was successfully utilized as a template for metal nanowire formation (Fig. 4A) (4, 83–86). The obvious advantages of such dipeptide-based nanotubes are their ease of synthesis and biodegradability. These peptide nanotubes could be produced in large scale without significant cost, and their degradation could be further modified using D-amino acids. Phe-Phe nanotubes can be formed by vapor deposition method and can self-assemble in aqueous solution (87). Therefore, using these kinds of dipeptide templates and their strong tendency to Nanomaterials: amyloids reflect their brighter side Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing evidence indicates that amyloids may also perform native functions in host organisms. Discovery of such amyloids, referred to as functional amyloids, highlight their possible use in designing novel nanostructure materials. This review summarizes recent advances in the application of amyloids for the development of nanomaterials and prospective applications of such materials in nanotechnology and biomedicine. Keywords: Nanotechnology, self-assembly, peptide/protein, fibrils, tissue engineering, stem cells, drug delivery, nanowires................ ................The amyloid forming capabilities of NM domain of the yeast Sup35p was successfully used for constructing metal nanowires that were able to conduct electricity with low resistance.................................... ..............Enhancement of desired properties of conducting materials can also be achieved using peptide nanotubes and fibrils. For example, Yemini et al. reported that the electrochemical properties of graphite and gold electrodes could be improved with the help of peptide nanotubes, when they were directly deposited on the electrode (88). This technique could be useful for the development of (bio)sensors with high analytical performances. Integrating amyloid fibers and polymers can lead to novel nanocomposite materials with high performance of material properties. Herland et al. integrated semi-conducting conjugated oligoelectrolytes with [/quote] www.ncbi.nlm.nih.gov/pmc/articles/PMC3215191/another snippet:============================ www.ncbi.nlm.nih.gov/pmc/articles/PMC3215191/figure/F0001/?report=objectonly************************************* image:
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Post by skyship on Nov 12, 2013 3:20:07 GMT -5
amyloids used in bionanotech. Makes the network for the interface and they are charged nanowires inside the amyloid.
nanotubes are smaller. and they interact too.
So virus used first, then prion itself, then the nanoparticle. All mutate into the cells, but start as monomers, bottom up, matter physics as well.
It is a conducting nanowire, how can it be soluable? sup35 prions are from fungus. So we have fungus, prions forming amyloids with nanowires conducting the light show. M13 virus.
So we have Viral phage that replicates, prions that replicate, amyloids that keep on growing and then along comes the nanoparticle in the buckyball cage forming the hexs which make up the nanotubes.
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Post by skyship on Nov 12, 2013 3:26:38 GMT -5
Amyloid technology Developing novel and biocompatible scaffolds for applications in drug delivery, tissue repair/engineering and other nanotechnological devices is one of the key areas in modern science. Significant attempts have been made using bottom up approach with peptide/protein self-assembly to create functional biomaterials for applications LIL SIS.........here are the PEDOTS..........you are so right, my friend. Nanowire development using self-assembling peptide/proteins and amyloid fibrils. (A) The nanotubes made by the self-assembly of Phe-Phe dipeptide were utilized as a template to form silver nanowires (83). (B) Cysteine labeled amyloid was used to develop metal nanowires, by first covalently linking the nano-gold to surface exposed Cys residues, followed by silver ion reduction in solution to provide a silver coating, and subsequently making deposition of gold (39). (C) Insulin amyloid fibrils coated with alkoxysulphonate PEDOT-S was able to generate conducting nanowires (92). www.ncbi.nlm.nih.gov/pmc/articles/PMC3215191/figure/F0005/from the same article as above: www.ncbi.nlm.nih.gov/pmc/articles/PMC3215191/
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Post by skyship on Nov 12, 2013 3:41:34 GMT -5
In this case "insulin amyloid fibrils coated w/ alkoxysulphonate PEDOT-S and each of those generate conducting nanowires. Iron-Catalyzed Polymerization of Alkoxysulfonate-Functionalized 3,4-Ethylenedioxythiophene Gives Water-Soluble Poly(3,4-ethylenedioxythiophene) of High Conductivity Chemical polymerization of a 3,4-ethylenedioxythiophene derivative bearing a sulfonate group (EDOT-S) is reported. The polymer, PEDOT-S, is fully water-soluble and has been produced by polymerizing EDOT-S in water, using Na2S2O8 and a catalytic amount of FeCl3. Elemental analysis and XPS measurements indicate that PEDOT-S is a material with a substantial degree of self-doping, but also contains free sulfate ions as charge-balancing counterions of the oxidized polymer. Apart from self-doping PEDOT-S, the side chains enable full water solubility of the material; DLS studies show an average cluster size of only 2 nm. Importantly, the solvation properties of the PEDOT-S are reflected in spin-coated films, which show a surface roughness of 1.2 nm and good conductivity (12 S/cm) in ambient conditions. The electro-optical properties of this material are shown with cyclic voltammetry and spectroelectrochemical experiment reveals an electrochromic contrast (48% at λmax = 606 pubs.acs.org/doi/abs/10.1021/cm801512r?journalCode=cmatexpubs.acs.org/doi/abs/10.1021/ma047396%2B?journalCode=mamobxThis is the image of pedots with the thiophene: Saved this for a long time, from the "super soldier" materials creators.
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Post by skyship on Nov 12, 2013 4:15:23 GMT -5
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Post by skyship on Nov 12, 2013 4:28:40 GMT -5
the Amyloid connection: creating amyloidosis? Specifically, the spheres were made from N-tert-butoxycarbonyl (Boc)-protected diphenylalanine, which in unprotected form is the key ingredient in the beta-amyloid protein that facilitates plaques in the brain that form as a result of Alzheimer’s disease.Are these the nanospheres on the sides of the diphenylalanine the black spots labeled M and nPt?i.bnet.com/blogs/israel-strongest-nanosphere-material-102510.jpegSo, this N-tert butoxycarbonyl (Boc) is the protector? so one does not get amyloids? since it is same ingredient as the beta amyloid in AZ? I believe this would not be called Alz but a new form of introduced amyloid, that can either become unprotected by loss of shell and then initiates itself as a substituted amino acid. So, this new form would be the Morgellon form? Lil sis, It is an ESTER~! Keywords: Boc; dioxane; hydrogen chloride; selective deprotection; tert-butyl ester Abstract: Fast, efficient and selective deprotection of the tert-butoxycarbonyl (Boc) group of various amino acids and peptides was achieved by using hydrogen chloride (4 m) in anhydrous dioxane solution for 30 min at room temperature. In the cases studied in our laboratory, this protocol provided superior selectivity to deprotect Nα-Boc groups in the presence of tert-butyl esters and tert-butyl ethers, including thio-tert-butyl ethers, but not phenolic tert-butyl ethers. onlinelibrary.wiley.com/doi/10.1034/j.1399-3011.2001.00935.x/abstract?deniedAccessCustomisedMessage=&userIsAuthenticated=falsetert-butyl esters
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Post by skyship on Nov 14, 2013 1:49:19 GMT -5
Get out of the kitchen. these supplies must have the demon legions in them. bumping up this thread over the kitchen suppliers.
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Post by skyship on Nov 18, 2013 2:15:35 GMT -5
bumping up
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Post by skyship on Nov 23, 2013 17:39:45 GMT -5
What do we know about Oligomers? Prion Protein Fragment Hints At Infection MechanismStructural Biology: A small piece of the human prion protein forms oligomers with tails that could interact with healthy prions and convert them to infectious forms " Now researchers studying the crystal structure of a snippet of the human prion have found clues to how oligomers of the proteins could coax others to misfold ( J. Am. Chem. Soc. 2013, DOI: 10.1021/ja403001q) ",,,, ....." In the current study, Surewicz and postdoc Marcin I. Apostol decided to examine a 12-amino-acid portion of the human prion protein containing a disulfide bond. When they looked at these peptides’ structures, they found something surprising: Instead of forming twisting structures that look like amyloid fibrils, the peptides formed groups of hexameric oligomers rich with amino acids arranged in pleated β-sheets. It was an interesting finding, Surewicz says, because prion researchers have been debating whether the fibril structure or another oligomeric protein structure is the toxic prion species. Each oligomer has a tail consisting of amino acids in a β-strand that can form hydrogen bonds with neighboring peptides. The researchers suggest that these tails could explain how oligomer structures bind to and potentially perturb the structure of other peptides. Still, Surewicz cautions that it’s always dangerous to try to interpret the behavior of full proteins from the structures of parts. It’s an “intriguing and novel structure,” says Simon Sharpe of The Hospital for Sick Children in Toronto. Though the structure provides important insights into possible features of amyloid oligomers, he says, it’s unlikely that this particular structure will reflect the exact structure of full prion oligomers in a living organism."............ cen.acs.org/articles/91/web/2013/07/Prion-Protein-Fragment-Hints-Infection.html============ The hexagons we find could be these hexamers, and the created hsps could be the prions themselves, maybe called spitzenkorpers which seem to be present in certain fungi and yeasts, like s. cerevis. and podospora ansinera used in sup 35 and the nanowire, which is basically using the amyloid production as the filaments for the matrix.------------------------- Hexamer TroubleShort peptides from the human prion protein form hexamers (two views shown) held together with hydrogen bonds. Each individual peptide has its own color. cen.acs.org/content/cen/articles/91/web/2013/07/Prion-Protein-Fragment-Hints-Infection/_jcr_content/articlebody/subpar/articlemedia_0.img.jpg/1373979438279.jpg----------------------------- so, google and prions and amyloids, what do you think? Google nanowires?------------------------
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Post by lilsissy on Nov 25, 2013 22:15:47 GMT -5
which is cow conversion, cows that used to produce 4,000 gallons of milk each year now produce 40,000, if memory serves me right, the casein ( spell check needed has turned into B- Sheet Casein. arranged in pleated β-sheets www.ncbi.nlm.nih.gov/pubmed/21689790
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Post by jdp7100 on Jan 3, 2014 12:29:32 GMT -5
Good thread on prions. Here are energetic test results of myself which is important to post. It's the prion score that's important. img197.imageshack.us/img197/2976/1i6o.jpgFrom here www.royalrife.com/test_order.html (energetic test results or saliva test). There really aren't much in test results for prions but here is my energetic test results. When I was retested for prions, the score was 50 or 55 (I forget which). This is a "very" high number. Have a tendency for Parkinson's and cancer. When treating for prions, the score will fall and neurological symptoms greatly disappear. However, once stop treating for prions, the score rises again. The prions are shed from the skin allowing for self replication of morgellons fibers around the living areas of the home. Progress of morgellons can be monitored by collecting dust samples and observe under microscope. When morgellons/prions are high, just about everything in the dust sample are morgellons fibers. When morgellons/prions is low, the dust sample will have a much reduced number.
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Post by skyship on Jan 5, 2014 21:19:49 GMT -5
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Post by skyship on Jan 5, 2014 22:45:11 GMT -5
So they say these certain fibers are to be functional. Now, we know the prion unfolding in prions in the wild are not functional. But, they say these are. So, what is the purpose of this "pigment cell"? I have found info that will blow this out of the water, since they are somewhat non soluable. I need to get all the ducks in a row, so to speak. At first I thought HAC (aqt's link on Darpa) which still could be involved, and BAC, YAC and MAC: human artificial protein, bacterial artificial protein, yeast artificial proten and mammal artificial protein were the culprits, however, I tend to believe this created amyloid, not what is running rampart in the environment, as they say, which probably is and looks just like this created one, could be the culprit. However the created one involves pigment. Lil sis and I have thought melanin was involved. Also her sister showed prions as you do JDP~! How did you get he Prions tested? Special lab, blood, biopsy, serums etc? Jdp, Yes, so agree with you and I do think that I have a solution to prevent the formation of the fibers in the first place. Preventing high PH. by alkaline and the reason is, is that these form at 5.0 ph which is high in ph, the scale goes the other way. What is normal is around 7. If we have 11 on the scale that means the alkaline will prevent high ph and formation of these so-called "functional amyloids"...... My question is, could and many have done this, drink tsp of baking soda in 8oz of water, bring the alkaline high enough to prevent the formation of these filaments? I do use baking soda a lot and have some sores, but, not all over the body. If done everyday, I do wonder if this would bring the body back to normal state? The other think is what you mention. The Rife, and I think that and Priore machine, if we can find them, anymore would do this. Rife could take down the electrical fields around this, while even the Q-link magnetic apparatus could keep the magnetic fields around us normal as well, and inside as well. So, these 4 solutions, may work. The priore' machine is this: www.cheniere.org/books/excalibur/priore_machine.htmskyship
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Post by skyship on Jan 5, 2014 22:48:57 GMT -5
I see now you had an energetics test, saliva test.
How can we get these?
Skyship
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Post by jdp7100 on Jan 7, 2014 3:01:04 GMT -5
Hi Skyship, When you click on this link, www.royalrife.com/test_order.html scroll down to "The Electrical Patterns Test." From there, just have to print out the five links and send them in with $125 check and with two saliva samples. Then after a week or so will get the results in the mail with a small explanation of what the results mean. Then Dr. Loyd will call or you can call to discuss the results further and what can be done to lower the scores. I do very much believe that those with a high degree of morgellons fibers will also have a high prion score. I have spoken with someone else while they have never mentioned morgellons, he has seen a possible correlation to high viral scores and prions. I'm not sure how accurate but here is some interesting info: Prions and retroviruses: an endosomal rendezvous? “The authors speculate that retroviruses, perhaps endemic in certain flocks of sheep, might act as (presumably non-obligatory) co-factors in the infectious spread of prions.” www.ncbi.nlm.nih.gov/pmc/articles/PMC1500823/Virus in the frame for prion diseases "Viruses, not prions, may be at the root of diseases such as scrapie, BSE and variant Creutzfeldt-Jakob disease (vCJD), researchers say." www.newscientist.com/article/dn11168-virus-in-the-frame-for-prion-diseases.html#.UsuvgpuwmpEI should mention that high dose Vitamin C is recommended by a well known morgellons researcher. Note that high dose Vitamin C is a strong anti viral. However, morgellons needs an even stronger anti viral in my experience. It's theorized positive charge increase viral replication. Some interesting info = www.royalrife.com/powerlines.htmlNegative charge definitely inhibits viral replication. Pyroenergen were the first people to do this. Some info = www.pyroenergen.com/process.htm I have several DIY versions of this technology and is definitely very helpful for me as well as helpful for inhibiting cancer however there is a problem unique with morgellons I believe. Those with morgellons, the living environment contains an incredible amount of morgellons fibers. Once exposed to morgellons fibers, symptoms reappear. What is helpful to reduce symptoms for me is to have a very effective HEPA air cleaner called IQ Air Purifier. Unfortunately it costs $800. A P100 3M mask to clean the house with so as not to inhale the morgellons fibers when dusting the house is also important as well. Otherwise, when dusting, symptoms reappear all over again. Also, I have used a very powerful negative ion generator which is said to produce no ozone and interestingly it appears to reduce morgellons fibers replication in the room that it's placed. Although, this last one is not needed and low on my list of importance but always nice to have as it does appear to reduce morgellons fibers in the room it's in. www.amazon.com/Wein-Density-Negative-Air-Ionizer/dp/B000CECSYA/ref=sr_1_1?ie=UTF8&qid=1389081278&sr=8-1&keywords=negative+ion+generator
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Post by jdp7100 on Jan 7, 2014 14:45:26 GMT -5
Yes, so agree with you and I do think that I have a solution to prevent the formation of the fibers in the first place. Preventing high PH. by alkaline and the reason is, is that these form at 5.0 ph which is high in ph, the scale goes the other way. What is normal is around 7. If we have 11 on the scale that means the alkaline will prevent high ph and formation of these so-called "functional amyloids"...... My question is, could and many have done this, drink tsp of baking soda in 8oz of water, bring the alkaline high enough to prevent the formation of these filaments? I do use baking soda a lot and have some sores, but, not all over the body. If done everyday, I do wonder if this would bring the body back to normal state? The other think is what you mention. The Rife, and I think that and Priore machine, if we can find them, anymore would do this. Rife could take down the electrical fields around this, while even the Q-link magnetic apparatus could keep the magnetic fields around us normal as well, and inside as well. So, these 4 solutions, may work. The priore' machine is this: www.cheniere.org/books/excalibur/priore_machine.htmHi Skyship, A quote Many years ago I experimented with adding baking soda to water as well as adding very small amount of borax to water as well based on recommendations from earthclinic.com. It did help my symptoms but wasn't enough for me and I moved on. I can only assume and only a guess it wasn't able to inhibit prions elsewhere in my body. Outside the GI tract. Regarding PrPC and PrPSc, I once tried experimenting under a microscope with manganes oxide but was hard to verify what actually happened. I could have sworn but it appeared that some colored filaments were more susceptible to breaking up than others. It appeared the red morgellons filaments broke up into appears but hard to make out. Making me wonder if some colored filaments are PrPC and others PrPSc... FWIW, magnanese oxide can be found by breaking open a button battery. Then just add a little water and the black manganese oxide from the button battery to the morgellons filaments sample and observe under microscope.
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Post by jdp7100 on Jan 7, 2014 14:49:19 GMT -5
For those who wish to experiment under microscope, here is additional information regrading how to degrade and inactivate prions. Note Clifford Carnicom's method of sodium hydroxide and it's use in other studies regarding prions. -------------------------------------------------- It has been discovered that it is possible to treat solutions of connective tissue material for the inactivation of prions in a manner such that connective tissue molecules are not adversely affected by the inactivation treatment. For example, solubilized atelopeptide collagen can be treated with sodium hydroxide for the inactivation of prions and other infectious agents without affecting the ability of the solubilized collagen to form stable fibers www.google.com/patents/US5756678------------------------------------------------- The use of NaOH can effectively reduce prion levels in an in vitro inactivation assay. After pretreatment of SBH with detergent, NaOH completely eliminates the PrPRES signal. Detergent may liberate lipid membrane-protected PrPSc to improve access to NaOH, which can then inactivate PrPSc by altering its structure. In cases of unidentified exposure to PrPSc during manufacturing, sanitizing procedures combining the use of detergent and NaOH may help to ensure minimal levels of contamination carryover in products. www.ncbi.nlm.nih.gov/pubmed/16756599------------------------------------------------ Photograph of the chemical method established to break down the outer shell of the filament and to access the contents of the filament. The method uses a combination of concentrated sodium hydroxide, concentrated potassium hydroxide and heat in a boiling water bath. Note the separation of colors within the solution within the test tube, one yellowish and one a deep red color. These colors represent different chemical and structural components of the filament. Approximately 45 minutes are required at boiling temperature to complete the separation. www.carnicominstitute.org/articles/penetration_of_filament.htm------------------------------------------------ Decontamination Methods for Prions www.memphis.edu/ehs/pdfs/deconprions.pdf
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Post by skyship on Jan 11, 2014 0:32:13 GMT -5
updating
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Post by skyship on Jan 11, 2014 2:48:03 GMT -5
updating Important Info
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