Betreff: Protein folding as relates to changes in energy....VIP...2004
Datum: Fri, 8 Jul 2005 12:40:20 EDT

Dear Dr. Uckun:  Protein folding problems are currently a "high priority" area of U.S. Gov't research.   Would you please advise whether or not Parker-Hughes and/or Wayne Hughes Institute is conducting protein folding/amyloid research at this time?   If so, is some or all of this work funded by NIH, H&H, DOD or some other branch of the government?   If Parker-Hughes/Wayne Hughes Institute is not involved in protein folding research, would you please advise as to whether or not any Leukemia-electromagnetic radiation research is currently being done?
One of my guinea pigs (exposed chronically to low levels of EMR -- electric meter) initially having mostly "hypersegmented neutrophils" identified by CBC with diffs, soon followed by severe neutropenia and lymphocytosis with improving CBC's/diffs after reduction of EMR exposure, died from Reactive Renal Amyloidosis a couple of years later.
 Amyloid is related to heat shock protein effects/"environmental stress proteins" due to protein misfolding, etc.   I emphasize the "environmental stress definition" primarily because of all the controversy surrounding "thermal issues."   The term "heat shock" is really a matter of "environmental stress" that doesn't require temperature changes.. 
As you reported back in 1999, "the BTK Gene" is responsible for immune deficiencies as well as Leukemia.   Your work re the BTK Gene involved EMF research.   Conclusions of EMF RAPID confirmed a connection to low levels of EMF's and childhood Leukemia.
There are published studies regarding a connection between amyloid and Leukemia and, as you know, the 2002 EMF California Report has linked brain cancer, Leukemia, Lou Gehrig's Disease and miscarriage to EMF levels as low as 4.0 mg.   Amyloid is involved in countless other diseases including Type II diabetes, Alzheimers.  Amyloid precursor protein appears to be involved in the development of M.S.
Assoc. Prof. Olle Johansson of the Karolinska Institute's Dept. of Neuroscience, in Sweden, has offered to replicate findings re my guinea pigs (all four developed "hypersegmented neutrophils," severe neutropenia and lymphocytosis soon after "powerwall/electric meter exposures" -- asthma was an early symptom).    Dr. Johansson has also agreed to do studies replicating the rare immune deficiencies in two of my grandsons (IgG subclasses 1 and 3 indicate "ageing") that occurred as result of sleeping against walls opposite electric meters in their respective homes. 
While awaiting word from Children With Leukaemia in London re my request for funding Dr. Johansson's work, it has occurred to me that if you, Parker-Hughes and/or Wayne Hughes Institute are currently involved in protein folding research and/or electromagnetic radiation research re Leukemia, that you are in a position to do a confirmatory study or studies.
I would be glad to provide copies of lab reports and other information regarding my two grandsons as well as veterinary reports re my guinea pigs and any other information regarding exposure conditions.   Confirmatory studies should yield straightforward, uncomplicated, drastic changes both from standpoint of harmful health changes as well as much-improved health after subject(s) are removed from close proximity to EMF source (electric meter, electric clock radio, etc.).
We were never told by the boys' immunologist that you are/were "an EMF researcher," however, we were told you were researching immune problems while at the University of Minnesota.  Later, blood from at least one of my grandsons was sent to the Wayne Hughes Institute.   Asthma and sinus infections were chronic symptoms in both grandsons.
At some later time, the immunologist did report that "a candidate gene was found that is the same for hypogammaglobulinemia (low immune) as that for Leukemia.  No other comments were made by the immunologist except for his initial response to questions re EMF exposure,   ".....some studies indicate immune changes in mice exposed to EMF's, however, we don't know how much of what happens to mice happens to people.......[not verbatim]......" 
I have made several pleas to Parker-Hughes Cancer Center (sent to your attention) for help to begin to inform the public that electric appliances should be removed from close proximity to beds.  Considering the relationship between the development of amyloid, plus all of the information re harm being done by "inflammation," AND the fact that you, as head of Parker-Hughes, are a major EMF researcher with information about confirmatory connections, my request for some sort of a pamphlet and hopefully public service announcements, does not seem to be unreasonable.     Any electrical item that has a power supply such as a cordless phone, telephone answering machine, etc. is also a concern if close to the head of a bed (possibly as close as 3 ft.).
I would be glad to send you a copy of the "U.S. News" article the American Cancer Society sent to me back in 1994 that recommends removal of electric appliances from bedsides.  Likewise, the EMF booklet that was prepared by utilities' communications' experts in 2001 that suggests " may want to replace electric clocks in bedroom with battery-operated or windup clocks.......[not verbatim]....."
Since our government is involved in game-playing, concealing, minimizing, etc. and "an insider" informed "Microwave News" that the EMF Interagency Committee Report may never be presented to Congress, the responsibility falls on those of us who know while continuing to put pressure on politicians to take responsibility in this urgent matter!!!!
Take care  -   Joanne
Joanne C. Mueller
Guinea Pigs R Us
731 - 123rd Avenue N.W.
Minneapolis, Minnesota  55448-2127  USA
Phone:   763-755-6114

Betreff: Protein folding as relates to changes in energy....VIP...2004
Datum: Mon, 4 Jul 2005 14:18:44 EDT

Protein energy profiles offer clues about amyloids

06 Oct 2004   

Patients suffering from diseases as varied as Type II diabetes, Alzheimer's, Parkinson's and dozens of lesser known maladies have one thing in common: they suffer from a large build up of amyloids, tissue that's created when millions upon millions of misfolded proteins stick together and form a mass that the body can't get rid of on its own.

Doctors don't yet understand whether amyloids cause disease or result from it, but the fact that they are present in very different diseases affecting millions of people points to the need for improved understanding of the basic processes of protein folding, one of the most complicated and least understood of all biological phenomena.

Research appearing in the Oct. 8 issue of the Journal of Molecular Biology, describes a new technique that may help scientists predict which proteins are prone to misfold and at what point the folding process is likely to break down. The research could support efforts to find the causes for diseases involving amyloids, and it could prove useful for researchers studying proteins involved in even more prevalent diseases like cancer and heart disease.

"We know now that most diseases involve proteins going wrong in one of two ways," said lead researcher Cecilia Clementi, assistant professor of chemistry at Rice University. "In the first, proteins don't function correctly because they fold into the wrong shape. This is something we see in sickle-cell anemia, for instance, because of genetic flaws that cause the amino acid sequence to be incorrectly synthesized.

"The second way proteins go wrong is by not folding at all, which is what we find in diseases involving amyloids. In these situations, the misfolded proteins assemble together into macroscopic aggregates."

All the basic functions of life are carried out by proteins, and the DNA in each of our cells contains the blueprints for all the proteins we need. Every protein has a characteristic shape, and it folds itself into that shape very soon -- generally in less than a second -- after it is made. To carry out their tasks, proteins interact with one another, bind with some molecules, cleave others into pieces and fuse other molecules together.

Since the function of a protein is often based upon specific chemical interactions -- enzymes, for instance, are proteins that make or disrupt chemical bonds in other molecules -- individual atoms of a protein must be aligned just so if they are to function properly. Consequently, there is a direct relationship between a protein's shape and its function.

The study of amyloids is complicated by the fact that the shape of very few proteins is known, the mechanics of protein folding are a mystery, and protein folding is incredibly complex; even the fastest supercomputer in the world would take decades to simulate all of the chemical interactions that take place when a single protein folds itself into its characteristic shape.

Despite this mystery and complexity, Clementi and colleagues believe they are creating a statistical method that will help scientists predict which proteins are prone to misfold.

"In designing a computer model for protein folding, you can't take everything into account because there are too many variables," said Vijay Pande, assistant professor chemistry and of structural biology at Stanford University and founder of the Folding@Home distributed computing project. "By designing simplified models that retain the essential physical and chemical features of protein dynamics, Clementi's team is making excellent progress in quantitative prediction -- work that's highly complimentary to the detailed simulations we're creating through Folding@Home."

Basic thermodynamics dictates that the entire process of protein folding can be seen as the systematic progression of the unfolded protein into its lowest possible free energy state. To identify whether a protein is a candidate for misfolding, Clementi has devised a dynamic interplay between theory and experiment -- with each informing the other as an experiment is carried out -- to construct a profile of the energy states a protein progresses through while it folds.

When this energy profile is plotted on a multidimensional graph, Clementi and her colleagues study the image like a mountain range, looking for low-lying valleys -- reduced energy states where the protein is most likely to become sidetracked before it can finish folding into its proper shape.

Ultimately, Clementi hopes the technique will be refined and used to catalog the folding energies of proteins that have already been implicated in specific diseases. She believes the profiles could offer new clues to doctors and drug companies about which proteins are good candidates for drug therapy.

Clementi co-authored the latest study with graduate student Silvina Matysiak. Two other graduate students in Clementi's group, Payel Das and Alexei Tcherniak, and undergraduate student Yoav Kallus, are working with Clementi and Matysiak to test and improve the technique for practical applications.

The research is sponsored by the National Science Foundation, the Welch Foundation and the Texas Advanced Technology Program.

Contact: Jade Boyd
Rice University