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Post by skyship on Feb 12, 2014 19:29:29 GMT -5
But there were other capacitors in between the idea and the final nano. plenty: evomech4.blogspot.com/feeds/posts/default?orderby=updated====================== METHYLATION of cytosine is a common DNA modification widely distributed in both prokaryotic and eukaryotic kingdoms. Cytosine methylation is an important epigenetic mark that modifies the information content of the underlying genetic sequence. Perturbation of cytosine methylation, in mutants or by inhibitor treatment, leads to developmental defects in organisms ranging from plants and fungi to mammals www.genetics.org/content/162/1/355.fullSo methylation is one strategy used to activate these variations so they can be seen but will produce defects. You are activating the inactive hidden in the DNA so called Junk, not junk at all, there for a reason.
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Post by skyship on Feb 12, 2014 19:37:45 GMT -5
Now, under the light of variations rather than origin of species, we can see where this went. Recent work on the heat-shock protein Hsp90 by Rutherford and Lindquist (1998) has been included among the pieces of evidence taken to show the essential role of developmental processes in evolution; Hsp90 acts as a buffer against phenotypic variation, allowing genotypic variation to build. When the buffering capacity of Hsp90 is altered (e.g., in nature, by mutation or environmental stress), the genetic variation is "revealed," manifesting itself as phenotypic variation. This phenomenon raises questions about the genetic variation before and after what I will call a "revelation event": Is it neutral, nearly neutral, or non-neutral (i.e., strongly deleterious or strongly advantageous)? www.academia.edu/547283/Hsp90-induced_evolution_adaptationist_neutralist_and_developmentalist_scenarios
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Post by skyship on Feb 12, 2014 21:07:52 GMT -5
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Post by skyship on Feb 12, 2014 21:39:11 GMT -5
So, deliberately, disease increases. By changing the environment you accomplish this, or by using the natural changes in environment, the upcoming Ice Age which happens every 11,000 years, you use this as an advantage to weed out those who cannot adapt to the variable.
Again:
So, from Global Warming.....to Climate Change....to GeoEngineering....you are changingng the environment.
And this is accidental, natural or imposed upon us?
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Post by skyship on Feb 12, 2014 22:21:13 GMT -5
====================================
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Post by skyship on Feb 12, 2014 22:28:29 GMT -5
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Post by skyship on Feb 13, 2014 13:23:36 GMT -5
It seems the heat shock proteins and now cold shock proteins from collembola(or snow fleas) can be vectors of this initiation. These seem to be the origin of either extreme good health or increased variations which then cause a dis-ease state. These were dumped on West coast and Minnesota recently with the snow. But, it seems they were dumped by Military plane and then chemtrails after. They were in the snow. www.youtube.com/watch?v=tdYU49rmLhYOr could they be cold shock proteins to keep animals alive? These proteins are found in collembola, and was this the insect used for the mu and lambda inserting the heat shock and cold shock proteins. These would then be evolutionary events. Here is a report saying how 2 cold shock proteins were found in collembolas. There should be a good reason for dumping them, right? The eggs of these collembolas are very hearty. So, when the Cold Spring arrives, will these be hatching everywhere? In soil and snow as it melts? Antifreeze proteins. Found in plants and environment. Antifreeze proteins. Prevents animals from freezing, maybe humans too? create the heat, cold or whatever, dump the fleas to prevent freezing. One with nature~!"We purified antifreeze proteins from winter-active snow fleas, Hypogastrura harveyi. These 6.5- and 15.7-kilodalton thermolabile proteins are glycine-rich (45% of the residues), and the short isoform is composed of the tripeptide repeat Gly-X-X. This makes them very different from other antifreeze proteins, including two from insects, suggesting independent adaptation to freezing environments. " www.sciencemag.org/content/310/5747/461.abstract Since hsp 90 is an evolutionary capacitor, would cold shock proteins work the same way? found in foods and environment, because they have a purpose. This time found in insects. Small is better they say, like in nano.
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Post by skyship on Feb 13, 2014 13:47:46 GMT -5
Classifications etc: Collembola. www.collembola.org/index.htmlHypogastrura harveyi. bugguide.net/node/view/370560Well well..................... New insights into ice growth and melting modifications by antifreeze proteins Maya Bar-Dolev 1 , Yeliz Celik 2 , J. S. Wettlaufer 3,4 , Peter L. Davies 5 and Ido Braslavsky* ,1,2 1 The Robert H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Jerusalem, Israel 2 Department of Physics and Astronomy, Ohio University, Athens, OH, USA 3 Yale University, New Haven, CT 06520-8109, USA 4 NORDITA, Roslagstullsbacken 23, 10691 Stockholm, Sweden5 Department of Biomedical and Molecular Sciences, Queen’s University, Kingston, Ontario, Canada Antifreeze proteins (AFPs) evolved in many organisms, allowing them to survive in cold climates by controlling ice crystal growth. The specific interactions of AFPs with ice determine their potential applications in agriculture, food preservation and medicine. AFPs control the shapes of ice crystals in a manner characteristic of the particular AFP type. Moderately active AFPs cause the formation of elongated bipyramidal crystals, often with seemingly defined facets, while hyperactive AFPs produce more variedcrystal shapes. These different morphologies are generally considered to be growth shapes. In a series of bright light and fluorescent microscopy observations of ice crystals in solutions containing different AFPs, we show that crystal shaping also occurs during melting. In particular, the characteristic ice shapes observed in solutions of most hyperactive AFPs are formed during melting. We relate these findings to the affinities of the hyperactive AFPs for the basal plane of ice. Our results demonstrate the relation between basal plane affinity and hyperactivity and show a clear difference in the ice-shaping mechanisms of most moderate and hyperactive AFPs. This study provides key aspects associated with the identification of hyperactive AFPs. Keywords: ice-binding proteins; melting shapes; ice-structuring proteins; crystal growth; antifreeze proteins; hyperactive antifreeze proteins rsif.royalsocietypublishing.org/content/early/2012/07/06/rsif.2012.0388.full.pdf==================== So now we have HSPs and AFPs..........
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Post by DonZ on Feb 14, 2014 18:14:33 GMT -5
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Post by skyship on Feb 14, 2014 23:17:35 GMT -5
DonZ, coinfections are one thing, but, Morgellons can be infection free, we have found this, meaning this is not related to gmo foods, where agro and the bartonella t4ss is a secretion system that sets itself up when we eat gmo foods. If we do not eat them, we are less likely to get this. You have the GMO part of this down solid. There is is more and that involves the field releases in the environment itself, in the wild. There are domestic illness and there are wild environmental issues. We have crossed paths, and I want you to know you have the the genetically modified organisms parts down. as does Schaller. Yes, same info in Germany. We are on the same page, I am just a few pages down from you into the inorganic nano. and it is there, for I have found the telechelic polymers, they are not natural. I know there is more involving the insecticides, but there is an even more advanced form. and this involves nano. Nano particles are an easier delivery vehicle or vector, and they self assemble. This is being hidden, but, if one looks hard enough and long enough you start to see the overall picture. You have one corner of this puzzle. and yes, I do agree that your protocol may be the best so far. as is jdp's if one wants to use the rife and get to the frequencies for that is what involves the nano smart materials. DonZ, You have found the T4SS secretion system tool used on humans. It was done with bug vectors, all that Schaller mentioned. I so agree. Many have gotten past this as you have, now watch for the nano. In fact would you try this? www.youtube.com/watch?v=usp962NKLboEven if you have cured the organic part, would you try this to see if you still have these filaments? You may have integrated them through the artificial immune system phase of your protocol? not sure. But, if you cannot do wine, use grape juice, freq are same for the organism, and you will see branching tree like structures, not the forms shown in the wine test. I believe the grape juice brings out the entire element. If one has pain in the gums, swishing with warm water added to the grape juice will bring these things out, and the pain will stop. I have done this over and over. The grape juice pulls them out, have put grape juice on lesions and has pulled out these organic and inorganic filaments. Also, I have a link to what Morgies find also: Hexagons. I believe I have found the hexagons, and there are also FRETS used as biosensors in every living thing. They work like dopplar in tornadoes. Dopplar radar? Nanoparticles can do this now. They have gone quiet now with nano, and I think the final ritual is to be done. Somehow it involves palladium which is in nanoparticles, buckyballs and other nano products. Palladium is like gold, but, is not manna as they claim, it is a substitute. Powder gold heals people. Barium is in the Aerosol Operations: en.wikipedia.org/wiki/Palladium============================= So, this goes into physic my friend. Please take the test, let me know what you find. Swish with the grapejuice for the branched filament, and you will see it come out of your mouth, about 30 seconds for big pieces. If you have a few, do it a number of times. See if larger pieces come out. Thank you and know that I appreciate you~! Skyship
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Post by jdp7100 on Feb 15, 2014 3:10:45 GMT -5
Please take the test, let me know what you find. Swish with the grapejuice Hi skyship, For what it's worth, my protocol does not physically remove the filaments and will still show a high concentration in the grape juice test. What my protocol does is focus on preventing morgellons fibers replication. To deactivate so to speak. Temporarily. Does not destroy nor does it remove. I know of no method that can physically remove enough fibers from the body to recommend or to permanently deactivate the morgellons fibers. I assume all successful protocols for morgellons are similar. With that said, inhibiting prion replication can give 100% relief in my experience. Non healing lesions heal quickly, no future lesions appear and skin improves where texture is no longer rough. Acute and chronic ailments produce electrical patterns in the body that can both be measured and a counter-frequency induced to eliminate. Think of it as stopping quorum sensing.
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Post by jdp7100 on Feb 15, 2014 16:18:49 GMT -5
One more thing I should mention. I've mentioned it in the past but just in case it was overlooked, the most effective method to find if a protocol is working is by taking before and after dust samples from the living areas in the home and examine under a microscope. Before samples would show an incredible amount of morgellons fibers! After samples from an effective protocol should show the living areas containing very little morgellons fibers.
This also works for taking before and after samples of your hair brush as well.
It appears that shedding of skin cells in the living areas of the home and hair brush, that morgellons fibers are replicating from the skin cells. Inhibiting prions prevents the morgellons fibers from replicating. Meaning, morgellons fibers are not replicating from the skin cells any longer.
Remember that prions are found in the skin as well as the tonsils and other areas of the body.
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Post by skyship on Feb 16, 2014 2:17:00 GMT -5
Jdp said....... . So by stopping the prions from activating stops the replication. Okay, so these replicate from skin cells. Just found something on Cutaneous Deposition Diseases and link to Xanthophyll lutein esters. Could be where the waxy stuff comes from. When the waxy is removed after hot shower or bath, then the mucus type stuff comes out and then finally the filament in Morgellons. It seems there are also besides wax, mucus and filaments, black specks left as well, this could be caron related as in carbon nanotubes. These seem to connect to cells in connective tissue and prions travel down them. That one is a new one on me. tunnelling nanotubes, and these are supposed to be natural.......not originating from humans~! delivered by nanoparticle, or chemical signal maybe? ========================================= ------------------------------- Cylindrins: We are onto the small oligomers, and there are larger ones as well. We do not get a good picture of the image: but here is the info on how they are formed:======= The cylindrins derived from ABC, an amyloid-forming protein, exhibit the properties of oligomeric state, immunoreactivity, and cytotoxicity commonly ascribed to small amyloid oligomers. (A) Ribbon diagram of a single subunit of ABC (16), colored by propensity to form amyloid, with red being the highest and blue the lowest propensity. The segment from residue 90 to 100, termed K11V, forms the cylindrin. www.sciencemag.org/content/335/6073/1228.figures-only================================== K11V forms the cylindrin: www.sciencemag.org/content/335/6073/1228.figures-only
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Post by skyship on Feb 16, 2014 2:39:14 GMT -5
Cylindrins: An anti-parallel slant. X-ray crystallography reveals that fragments of αB crystallin form an anti-parallel, β-barrel oligomer called cylindrin. Cylindrin does not appear to form stable fibrils akin to those assumed by Aβ and other amyloids linked to neurodegenerative diseases, but cylindrin poisons neurons and may be related to toxic Aβ oligomers. Image credit: Science/AAASwww.alzforum.org/sites/default/files/legacy/images/spotlight/large/EisenbergCylindrin_lg.jpgNow I do believe this fits the hsp104 motor. HSP were added over and over in foods and in the environment. There are 6 subunits and more.
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Post by skyship on Feb 16, 2014 2:57:13 GMT -5
Now lets look at the HSP 104 motor: Before I get into the hsp business, I would like you all to see this: This is a AFP or an antifreeze protein from the spruce budworm: it is called sbwAFP: It is a hexagon, the only one of the AFPs, although there are two from the Collembola. Notice the shapes.========================= ============================= =================================== What is interesting about these, is that they can be crystalized in the geo operations. As can the dump of the collembolas and their AFPs. And they can operate even if it is not cold once in the system.====================== Are our filaments, unfolded proteins like on the left? Right shows the conformation fold. Are these unfolded proteins bundled or aggregated into bundles? So, they may not be conforming to this new onslaught of programmed folding?en.wikipedia.org/wiki/Protein_folding==========================
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Post by skyship on Feb 16, 2014 13:31:46 GMT -5
DonZ, Another thing added to the gmo crops is RuBisCo. This is interesting in that it involves what is called "inorganic carbon". People say that doesn't exist. Then I wonder why it is used to alter foods or fix carbon as they say. Interestingly, D Eisenberg has done some work here. The same guy who was studying the cylindrins or small oligomers. I like to look at who created these names and what they mean, or who used their own name(s) to label them. History of the term RuBisCO See also Carbon cycle Photorespiration ======================= Pyrenoid en.wikipedia.org/wiki/PyrenoidExample of pyrenoids: Whether Rubisco self-assembles into pyrenoids or requires additional chaperones is at present not known. en.wikipedia.org/wiki/Pyrenoid=================================== C4 carbon fixation Crassulacean acid metabolism/CAM photosynthesis Carboxysome en.wikipedia.org/wiki/Rubisco
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Post by skyship on Feb 16, 2014 14:03:58 GMT -5
Some other terms I am looking into. I wonder if Pyrenoid is like prions, it is proteinaceous. Maybe they named it wrong, which is likely. Just create as you go along. Cylindrins were given that name as well. A created name but does describe the form of unfolded/folded proteins. A climate change avoidance strategy? en.wikipedia.org/wiki/C4_carbon_fixation=============== The whole geoengineering scenario involves Carbon. =========== Camphotosynthesis: again RuBisCO is used. Comparison with C4 metabolism CAM is named after the family Crassulaceae, to which Jade plant belongs en.wikipedia.org/wiki/Crassulacean_acid_metabolism==================== Malate? When rubisco first evolved, the inability of the enzyme's active site to exclude O2 would have made little difference. Now, it is considered to be wasteful, since photorespiration drains away as much as 50% of the carbon fixed by the Calvin cycle. If photorespiration could be reduced in certain plant species, without affecting photosynthetic productivity, crop yields and food supplies would increase. Alternative Strategies of Carbon Fixation - C4 and CAM C4 Plants The environmental conditions that promote photorespiration are hot, bright, dry days. In these climates, alternate modes of carbon fixation have evolved to minimize photorespiration. The two most important of these photosynthetic adaptations are exhibited by C4 and CAM C4 plants. C4 plants are so named because they form a four-carbon compound as the first product of the nonlight requiring reactions of photosynthesis. Several thousand species in at least 19 families use the C4 pathway. Agriculturally important C4 plants are sugarcane and corn, members of the grass family. Leaves of C4 plants contain two distinct types of photosynthetic cells: a cylinder of bundle-sheath cells surrounding the vein, and mesophyll cells located outside the bundle sheath. CO2 is initially fixed in mesophyll cells by the enzyme PEP carboxylase. A four-carbon compound is formed (malate in this case) which conveys the fixed CO2 via plasmodesmata (protoplasmic connections) into a bundle sheath cell where the enzymes of the Calvin cycle are located. C4 Leaf Anatomy In the bundle sheath cell, the malate is converted into pyruvate and CO2; the latter is now used by rubisco and the Calvin cycle to make sugar. Compared to rubisco, the enzyme PEP carboxylase has a much higher affinity for CO2. Thus, PEP carboxylase can fix CO2 efficiently when it is hot and dry and stomata are partially closed. Also, by pumping CO2 from the mesophyll cells into the bundle sheath, this keeps the CO2 concentration high enough for rubisco to accept CO2 rather than O2. In this way, C4 photosynthesis minimizes photorespiration and enhances sugar production. This adaptation is especially advantageous in hot climates with intense sunlight and it is where C4 plants evolved and thrive today. A second photosynthetic adaptation to arid conditions (as found in deserts) has evolved in succulent (water-storing) plants (including ice plants), many cacti, and representatives of other plant families. These plants close their stomata in the day and open them during the night, just the reverse of other plants. Closing the stomata during the day helps desert plants conserve water, but it also prevents CO2 from entering the leaves. At night, when the stomata are open, these plants take up CO2 and initially fix it into four-carbon compounds like malate. This mode of carbon fixation is called crassulacean acid metabolism, or CAM, after the plant family Crassulaceae, the succulents in which the process was first discovered. The photosynthetic cells of CAM plants store the malate formed in the night in their vacuoles until morning, when the stomata close. In the daytime, when the light reactions can make ATP and NADPH2 for the Calvin cycle, CO2 is released from the malate made the night before to become fixed into sugar in the chloroplasts. The above diagram compares C4 and CAM C4 photosynthesis. Both adaptations are characterized by initial fixation of CO2 into an organic acid such as malate followed by transfer of the CO2 to the Calvin cycle. In C4 plants, such as sugarcane, these two steps are separated spatially; the two steps take place in two cell types. In CAM C4 plants, such as pineapple, the two steps are separated temporally (time); carbon fixation into malate occurs at night, and the Calvin cycle functions during the day. Both C4 and CAM C4 are two evolutionary solutions to the problem of maintaining photosynthesis with stomata partially or completely closed on hot, dry days. However, it should be noted, that in all plants, the Calvin cycle is used to make sugar from carbon dioxide. On a global scale, this represents a prodigious amount of sugar, about 160 billion metric tons of carbohydrate per year. www.bio.umass.edu/biology/conn.river/photosyn.html
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Post by skyship on Feb 16, 2014 18:50:44 GMT -5
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Post by skyship on Feb 16, 2014 18:54:49 GMT -5
Ribose definition: Ribulose is a ketopentose — a monosaccharide containing five carbon atoms, and including a ketone functional group. It has chemical formula C5H10O5. Two enantiomers are possible, D-ribulose (D-erythro-pentulose) and L-ribulose (L-erythro-pentulose). D-Ribulose is the diastereomer of D-xylulose. Ribulose sugars are composed in the pentose phosphate pathway. They are important in the formation of many bioactive substances. For example, D-ribulose is an intermediate in the fungal pathway for D-arabitol production. Also, as the 1,5-bisphosphate, D-ribulose combines with carbon dioxide at the start of the photosynthesis process in green plants (carbon dioxide trap). A synthetic form of ribulose known as sucroribulose is found in many brands of artificial sweeteners. en.wikipedia.org/wiki/Ribulose==================
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Post by skyship on Feb 16, 2014 19:45:01 GMT -5
Whole article and references: Synthetic Rubisco duplicates CO2-binding photosynthesis, providing climate-fighting hopeAbstracted on: 18 January 2010 For the first time, scientists have succeded in synthesizing the enzyme Rubisco, the key protein in fixing carbon dioxide in plants. The researchers, from the Max Planck Institute of Biochemistry and the Gene Center of Ludwig Maximilians University (Munich), have published1 their work in Nature. Rubisco is a large protein consisting of 16 subunits, and its complex structure has kept it from being synthesized. The problem has been that with 16 subunits the risk of the wrong subunits to combine and form useless aggregates is very high. To overcome this, the scientists resorted to "chaperone chemistry", where they introduced molecular chaperones that only allow correct parts of the protein come together (simulating the role of chaperones in supervising the meetings of young couples in real life). The researchers showed that two different chaperone systems, called GroEL and RbcX, are necessary to produce the right three-dimensional Rubisco complex. The scientists are now working on modifying the artificial Rubisco to bond only with CO2 — the natural product also metabolizes oxygen, degrading its efficiency. They say that a CO2-enhanced product would improve crop yields, and be more efficient at capturing CO2 for climate mitigation. 1. Nature: Coupled chaperone action in folding and assembly of hexadecameric Rubisco
Related abstracts Research heats up on using charcoal to fertilize soils and sequester carbonFinancial Times | 28 February 2009 Biotechnologist questions feasibility of microalgae to capture CO2 in a Hamburg powerplantHamburger Abendblatt | 29 November 2007 A massive dust storm feeds plankton, captures CO2, and provides a geoengineering clueThe Sydney Morning Herald | 6 October 2009 New metal-organic framework efficiently captures CO2 at high outputs, and regenerates easilyProceedings of the National Academy of Sciences | 1 December 2009 Central Atlantic basaltic rock is perfect for storing carbon dioxide offshore, researchers sayProceedings of the National Academy of Sciences | 4 January 2010 Lifecycle analyses show biochars can profitably store carbon, generate energy and nourish soilsEnvironmental Science & Technology | 15 January 2010 Catalyst preferentially strips CO2, not O2, from air, offering hope for cheap carbon captureNature | 14 January 2010 Alaska lottery to predict when the ice breaks offers geophysicts rare, reliable climate historyThe Wall Street Journal | 7 March 2008 US conference examines geo-engineering of the atmosphere to reduce global warmingThe American | 30 June 2008 New York tree census values the energy savings of the city’s 600,000 trees at $28 millionThe Economist | 5 July 2007 factclipper.com/abs/science/carbon-capture/2010-01-18/synthetic-rubisco-duplicates-co2-binding-photosynthesis-providGroEL.....and RbcX...... involve the chaperones. Here is where capacitors and heat shock and cold shock proteins come in the picture on a grand or global scale.
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Post by skyship on Feb 16, 2014 19:57:04 GMT -5
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Post by skyship on Feb 16, 2014 20:10:22 GMT -5
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Post by skyship on Feb 16, 2014 21:09:11 GMT -5
One can get a view of the discussions that should have taken place, but didn't from above papers and thoughts. but, this is the kicker: dric.nrct.go.th/bookdetail.php?book_id=119341well at least you can get the titleGroEL works with RuBisCO. but look what it does..... It may not be the hsp104 motor, but it has a lot of chaperoning going on. Unfolding and folding in a non native, polypeptide. GroEL chaperonin system. It unfolds proteins.......================= www.ncbi.nlm.nih.gov/pubmed/9759498========================== Now, can you see the connection to the chemtrails, and field releases? These could be done very small areas, just watch the generations. I have seen people monitoring these, in marshes etc and taking algae, red algae which is dangerous and very unhealthy, and this used in this geoengineering. CDC was seen checking it out on certain lakes. Just to see if it effect boaters. ========================== Not just aerosol operations, but field releases. Botanists know how this works and how it can spread rapidly without any spraying. 2 diverse unrelated observations concerning RuBisCO, chaperonins and Bacterio-phages.======================================= ======================== Here the observations start to tell the story of chaperonins (hsp60 for one) lambda, T4phage and others, and that GroEL is similar or the same as RuBisCO. So, changing crops, humans, animals, the wild etc.============================== He even calls it a nanomachine.......quoting from above link:======================================= reference 7: . ......"and with our demonstration in 1989 of what it was the chaperonin proteins really do".......
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPIn vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded poly-peptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hspGO) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E coli(groES), and Mg-ATP. Because chaperonins are ubiquitous, a conserved Mg-ATP-dependent mechanism exists that uses the chaperonins to facilitate the folding of some other proteins.www.nature.com/nature/journal/v342/n6252/abs/342884a0.htmlI will try to find the entire paper, if I can....
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Post by skyship on Feb 16, 2014 23:00:45 GMT -5
The author also references 14 and 16 from the Personal Observation story: Thirumalai D, Lorimer GH (2001) Ann Rev Biophys Struct Biol (in press) and www.nature.com/nature/journal/v342/n6252/abs/342884a0.html================= Now, this is peaking my interest: ===================== Assembly chaperones: a perspective Abstract The historical origins and current interpretation of the molecular chaperone concept are presented, with the emphasis on the distinction between folding chaperones and assembly chaperones. Definitions of some basic terms in this field are offered and misconceptions pointed out. Two examples of assembly chaperone are discussed in more detail: the role of numerous histone chaperones in fundamental nuclear processes and the co-operation of assembly chaperones with folding chaperones in the production of the world's most important enzyme. rstb.royalsocietypublishing.org/content/368/1617/20110398.abstractSo, we continue with the observations gang~!~!~! Hard to take in sometimes, but, you see what is going on. We are not done yet. S molecular chaperones self-assembly assembly chaperones Rubisco histone chaperones
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Post by skyship on Feb 16, 2014 23:06:02 GMT -5
that enzyme is a large oligomer. Please digest this slowly, as we need to do, since these obstruct natural enzymes from doing their jobs. We are now in the realm of the so called induced heat shock proteins and more. =================================== ******************************************************** rstb.royalsocietypublishing.org/content/368/1617/20130091.full
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Post by skyship on Feb 17, 2014 2:04:30 GMT -5
rstb.royalsocietypublishing.org/content/368/1617/F1.medium.gifCover image: Getting hot under the collar with sHSPs. The small heat-shock protein, MjHSP16.5 from the archael prokaryote, Methanocaldococcus jannaschii, is unphased by elevated temperatures (top row). However, the introduction of the R107G substitution (bottom row), which is equivalent to the iconic R120G disease-causing mutation in CRYAB, causes a significant increase in the dimensions of the reconstructed particle as computed from cryoelectron microscopy data using crystallographic data sets (bottom left). The relaxation in the structural constraints about the dimer–dimer interface due to the loss of the electrostatic interaction between R107 in one monomer and E98 in another has functional consequences. At these elevated (physiological) temperatures, R107G MjHSP16.5 is a better chaperone. (Cover image designed by Fei Sun and Yan Zhang, Institute of Biophysics, Chinese Academy of Sciences, and created by Yang Zhang, Ultra Digital Studio, China.) rstb.royalsocietypublishing.org/content/368/1617.cover-expansion
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Post by skyship on Feb 17, 2014 2:45:18 GMT -5
Expansion and compression of a protein folding intermediate by GroEL. Abstract The GroEL-GroES chaperonin system is required for the assisted folding of many essential proteins. The precise nature of this assistance remains unclear, however. Here we show that denatured RuBisCO from Rhodospirillum rubrum populates a stable, nonaggregating, and kinetically trapped monomeric state at low temperature. Productive folding of this nonnative intermediate is fully dependent on GroEL, GroES, and ATP. Reactivation of the trapped RuBisCO monomer proceeds through a series of GroEL-induced structural rearrangements, as judged by resonance energy transfer measurements between the amino- and carboxy-terminal domains of RuBisCO. A general mechanism used by GroEL to push large, recalcitrant proteins like RuBisCO toward their native states thus appears to involve two steps: partial unfolding or rearrangement of a nonnative protein upon capture by a GroEL ring, followed by spatial constriction within the GroEL-GroES cavity that favors or enforces compact, folding-competent intermediate states. www.ncbi.nlm.nih.gov/pubmed/15469819/================================ www.ncbi.nlm.nih.gov/structure?Db=structure&DbFrom=pubmed&Cmd=Link&LinkName=pubmed_structure&LinkReadableName=Structure&IdsFromResult=2107319============ GroEL and the molten globule foldingintermediate non native intermediate, means it is not natural to human body.
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Post by skyship on Feb 17, 2014 8:45:53 GMT -5
Did the RuBisCO become a buckyball when it became artificial and with intelligence? I think so. Is not the buckyball described here?: Alien invasion hoax? Who really makes the spaceships as well?Our brains and bodies were back engineered. Any alien that came here just might be our ancestors. www.mccormick.northwestern.edu/news/articles/archive/2009-2012/article_849.html ======================================= They are containers: this is what we have. I never gave up on the buckyball because everything fits, and this is not new as is claimed here as of 2011. So the artificial RuBisCo GroEl and GroEs etc are in the buckyball. the spheres are there (fullerenes)the new carbon, the mj was used in GroEl, an archaean, the cage is made of hexagons and pentagons. the pentagon is the sugar (Oligomer). It is all there. the charges on the polymers work with the Supermolecular apparatus.
So, I began this looking for a hexagon,( carboxysomes of which there are many to make the buckyball), the archean used, (among others), the specks (carbon) the spheres, the fullerene, filaments(small oligomers, cylindrins) and charged filament(nanowire inside the created amyloids(the leader, the Large Oligomer).
I always wanted to be an artist, like Klee, this would be the only way of figuring out forms, these were not designed even by man, they were formed from self assembling particles of graphene, soot, fullerenes. From volcanoes, from carbon in the atmosphere. You see the universe already had them, but they were not man made.Skyship, eyes wide open, ears tuned to the sound of the trumpets; heralding the real Word~!
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Post by skyship on Feb 17, 2014 9:04:54 GMT -5
The Risks were there, but, they operate under the principle of "Cremation of Care".
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Evidently the polymer (polyvinyl, latex etc) were toxic, so the self assembling nano (prion) worked well as functional material........walks right into the ribosomes. This is why we now have RNA diseases, well....the COMMON FUND should be multiplied because there are many with toxic parts causing diseases mentioned from the chaperones, the ever watchful eye of the Word, our 3 letter DNAs and the mitochondria which identifies us, our differences, our variations.
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Post by skyship on Feb 19, 2014 3:59:09 GMT -5
Polymer nanosystems:
But,, evidently, they are toxic.
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