We need our Governments and Corperations to invest in solar technology, everyday that we do not collect or store energy from the Sun we are losing money and wasting current energy resources.Google has even gone solar but I remeber awhile ago watching a show on PBS in which Alan Alda “yea that Doctor from M.A.S.H. ” in which he was exploring solar power options and inventions around the World on a show dedicated to alternative energy resources and some guy in Germany invented a spray on version of a solar collector that would coat shingles that are put on Homes then the shingles would be solar collectors and unlike glass solar panels of today, that when a part of the glass breaks the whole panel is useless for collecting energy, with these you could drill holes in the shingles or rip it up, cut it, or whatever and the rest of whatever was left would still collect solar energy. With nano techonolgy a coating could be used to spray any thing including recyceled styrofaom and it would collect energy all day I choose styrophoam because it is going to be here on this planet for the next 500 plus years so would make a great collector. A way to collect moon light would be another great idea if it was at all possible. One more thing is everyone in just America went to the bathroom outside once a month and no not a number 2 nobody needs to step in that, it would save nearly 300 million gallons of fresh water each month, and if we all skipped a shower once a month we would save over 10 billion gallons of water each month. and do not get my started on doing laundry equastion unless you want more numbers.
Inactive enzymes entombed in tiny honeycomb-shaped holes in silica can spring to life, scientists at the Department of Energy’s Pacific Northwest National Laboratory have found.
The discovery came when they decided to salvage enzymes that had been in a refrigerator long past their expiration date. Enzymes are proteins that are not actually alive but come from living cells and perform chemical conversions.
To the research team’s surprise, enzymes that should have fizzled months before perked right up when entrapped in a nanomaterial called functionalized mesoporous silica, or FMS. The result points the way for exploiting these enzyme traps in food processing, decontamination, biosensor design and any other pursuit that requires controlling catalysts and sustaining their activity.
“There’s a school of thought that the reason enzymes work better in cells than in solution is because the concentration of enzymes surrounded by other biomolecules in cells is about 1,000 to 10,000 time more than in standard biochemistry lab conditions,” said Eric Ackerman, PNNL chief scientist and senior author of a related study that appears today in the journal Nanotechnology. “This crowding is thought to stabilize and keep enzymes active.”
The silica-spun FMS pores, hexagons about 30 nanometers in diameter, mimic the crowding of cells. Ackerman, lead author Chenghong Lei and colleagues said crowding is important because it induces an unfolded, free-floating protein to refold; upon refolding, it reactivates and becomes capable of catalyzing thousands of reactions a second.
The FMS is made first, and the enzymes are added later. This is important, the authors said, because other schemes for entrapping enzymes usually incorporate the material and enzymes in one harsh mixture that can cripple enzyme function forever.
In this study, the authors reported having “functionalized” the silica pores by lining them with compounds that varied depending on the enzyme to be ensnared â€” amine and carboxyl groups carrying charges opposite that of three common, off-the-shelf biocatalysts: glucose oxidase (GOX), glucose isomerase (GI) and organophosphorus hydrolase (OPH).
Picture an enzyme in solution, floating unfolded like a mop head suspended in a water bucket. When that enzyme comes into contact with a pore, the protein is pulled into place by the oppositely charged FMS and squeezed into active shape inside the pore. So loaded, the pore is now open for business; substances in the solution that come into contact with the enzyme can now be catalyzed into the desired product. For example, GI turns glucose to fructose, and standard tests for enzyme activity confirmed that FMS-GI was as potent or better at making fructose as enzyme in solution. OPH activity doubled, while GOX activity varied from 30 percent to 160 percent, suggesting that the enzyme’s orientation in the pore is important.
“It could be that in some cases the active site, the part of the enzyme that needs to be in contact with the chemical to be converted, was pointing the wrong way and pressed tightly against the walls of the pore,” Ackerman said.
To show that the enzymes were trapped inside the FMS pores, the team stained the protein-FMS complex with gold nanoparticles and documented the enzyme-in-pore complex through electron microscopy. A spectroscopic analysis of the proteins squeezed into their active conformation turned up no new folds, evidence that they had neatly refolded rather than been forcibly wadded into the pore.
Researchers are developing smart “nanocarriers” for drug delivery and diagnostics.
By Kevin Bullis
Using parts of living cells in a smart nanotechnology-based system, researchers in Switzerland have demonstrated a “nanocarrier” that can target specific types of cells and light up in response to conditions in their immediate environment.
The work is part of a growing effort by scientists worldwide to develop nano devices that can circulate in the bloodstream, slip stealthily past the body’s immune system, attach to cancer or inflammatory cells (an important ability in diseases such as atherosclerosis and arthritis), and deliver a deadly drug payload–destroying some of the toughest diseases without the often debilitating side effects that can accompany chemotherapy (see “Nanomedicine”).
Already, early versions of such nano-based treatments have been approved for breast cancer. But Patrick Hunziker, a physician at University Hospital Basel, and Wolfgang Meier, professor of chemistry at the University of Basel, are attempting to trigger the release of the drugs at more precise locations and at release rates adjusted to have the most effect on a particular disease.
Composed of peptides, the liquid self-assembles into a protective nanofiber gel when applied to a wound. Rutledge Ellis-Behnke, research scientist in the department of brain and cognitive sciences at MIT and Kwok-Fai So, chair of the department of anatomy at the University of Hong Kong, discovered the liquid’s ability to stop bleeding while experimenting with it as a matrix for regrowing brain cells in hamsters.
The researchers then conducted a series of experiments on various mammals, including rodents and pigs, applying the clear liquid agent to the brain, skin, liver, spinal cord, and femoral artery to test its ability to halt bleeding and seal wounds.
“It worked every single time,” said Ellis-Behnke. They found that it stopped the bleeding in less than 15 seconds, and even worked on animals given blood-thinning medications.
The wound must still be stitched up after the procedure; but unlike other agents designed to stop bleeding, it does not have to be removed from the wound site.
The liquid’s only byproduct is amino acids: tissue building blocks that can be used to actually repair the site of the injury, according to the researchers. It is also nontoxic, causes no immune response in the patient, and can be used in a wet environment, according to Ellis-Behnke. A paper outlining the findings is available online and will be published in the December issue of Nanomedicine.
Ellis-Behnke believes that first responders, say, on a battlefield or at a traffic accident, will save more lives with the nanosolution. Yet the most significant application may be in surgery, he says, especially on the liver and brain.
In fact, as much as half of the time during any operation is spent “doing some sort of bleeding control,” says Ellis-Behnke. Consequently, such a liquid could “fundamentally change the pace of the operation.”
Ram Chuttani, director of endoscopy and chief of interventional gastroenterology at Beth Israel Deaconess Medical Center in Boston and assistant professor of medicine at Harvard Medical School, is familiar with their research. “Where I see huge applications is in patients who present with gastrointestinal bleeding,” he says. “[Right now,] there’s no ideal agent to endoscopically manage gastrointestinal bleeding.”
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Folding@Home is a goal to understand protien folding, misfolding and related diseases
What is protein folding and how is folding linked to disease? Proteins are biology’s workhorses — its nanomachines. Before proteins can carry out these important functions, they assemble themselves, or “fold.” The process of protein folding, while critical and fundamental to virtually all of biology, in many ways remains a mystery.Moreover, when proteins do not fold correctly (i.e. “misfold”), there can be serious consequences, including many well known diseases, such as Alzheimer’s, Mad Cow (BSE), CJD, ALS, Huntington’s, Parkinson’s disease, and many Cancers and cancer-related syndromes.
You can help by simply running a piece of software. Folding@Home is a distributed computing project — people from through out the world downloadÂ and run software to band together to make one of the largest supercomputers in the world. Every computer makes the project closer to our goals.Folding@Home uses novel computational methods coupled to distributed computing, to simulate problems thousands to millions of times more challenging than previously achieved. Learn more about this great cause by visiting the website located on Stanfords website