KSU also holds classes at the Cobb Galleria Centre, Dalton State College, Appalachian Technical College and Dallas. Current enrollment is over 32,000 students.
Caltech has six academic divisions with strong emphases on science and engineering. Its 124-acre (50 ha) primary campus is located approximately 11 mi (18 km) northeast of downtown Los Angeles.
Although founded as a preparatory and vocational school by Amos G. Throop in 1891, the college attracted influential scientists such as George Ellery Hale, Arthur Amos Noyes, and Robert Andrews Millikan in the early 20th century. The vocational and preparatory schools were disbanded and spun off in 1910, and the college assumed its present name in 1921. In 1934, Caltech was elected to the Association of American Universities, and the antecedents of NASA’s Jet Propulsion Laboratory, which Caltech continues to manage and operate, were established between 1936 and 1943 under Theodore von Kármán.
Despite its small size, 32 Caltech alumni and faculty have won a total of 33 Nobel Prizes (Linus Pauling being the only individual in history to win two unshared prizes) and 70 have won the United States National Medal of Science or Technology. There are 112 faculty members who have been elected to the National Academies. In addition, numerous faculty members are associated with the Howard Hughes Medical Institute as well as NASA. Caltech managed $332 million in 2011 in sponsored research and $1.75 billion for its endowment in 2012. It also has a long standing rivalry with the Massachusetts Institute of Technology (MIT).
California Institute of Technology (Caltech) research articles from Innovation Toronto
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- Researchers Test Smartphones for Earthquake Warning – April 13, 2015
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- Printing the Metals of the Future – July 30, 2014
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A computer algorithm for analyzing time-lapse biological images could make it easier for scientists and clinicians to find and track multiple molecules in living organisms. The technique is faster, less expensive and more accurate than current methods — and it even works with cell phone images.
A new image analysis technique makes finding important biological molecules — including tell-tale signs of disease — and learning how they interact in living organisms much faster and far less expensive. Called Hyper-Spectral Phasor analysis, or HySP, it could even be useful for diagnosing and monitoring diseases using cell phone images.
Researchers use fluorescent imaging to locate proteins and other molecules in cells and tissues. It works by tagging the molecules with dyes that glow under certain kinds of light — the same principle behind so-called “black light” images.
Fluorescent imaging can help scientists understand which molecules are produced in large amounts in cancer or other diseases, information that may be useful in diagnosis or in identifying possible targets for therapeutic drugs.
Looking at just one or two molecules in cell or tissue samples is fairly straightforward. Unfortunately, it doesn’t provide a clear picture of how those molecules are behaving in the real world. For that, scientists need to expand their view.
“Biological research is moving toward complex systems that extend across multiple dimensions, the interaction of multiple elements over time,” said postdoctoral fellow Francesco Cutrale. He developed HySP with Scott Fraser
, Elizabeth Garrett Chair in Convergent Bioscience and Provost Professor of Biological Science. The work was done at USC’s Translational Imaging Center, a joint venture of USC Dornsife and USC Viterbi School of Engineering.
“By looking at multiple targets, or watching targets move over time, we can get a much better view of what’s actually happening within complex living systems,” Cutrale said.
Currently, researchers must look at different labels separately, then apply complicated techniques to layer them together and figure out how they relate to one another, a time-consuming and expensive process, Cutrale said. HySP can look at many different molecules in one pass.
“Imagine looking at 18 targets,” Cutrale said. “We can do that all at once, rather than having to perform 18 separate experiments and try to combine them later.”
In addition, the algorithm effectively filters through interference to discern the true signal, even if that signal is extremely weak — very much like finding the proverbial needle in a haystack. Recent technology from NASA’s Jet Propulsion Laboratory can also do this, but the equipment and process are both extremely expensive and time-consuming.
In research published Jan. 9 online by the scientific journal Nature Methods, Cutrale and Fraser, along with researchers from Keck School of Medicine, Caltech and the University of Cambridge in the United Kingdom, have used zebra fish to test and develop HySP. In this common laboratory model, the system works extremely well. But what about in people?
“In experimental models, we can use genetic manipulation to label molecules, but we can’t do that with people,” said Fraser. “In people, we have to use the intrinsic signals of those molecules.”
Those inherent signals, the natural fluorescence from biomolecules, normally gets in the way of imaging, Fraser said. However, using this new computer algorithm that can effectively find weak signals in a cluttered background, the team can pinpoint their targets in the body.
Different fluorescent light wavelengths reveal features of a zebra fish embryo. Photo courtesy of Francesco Cutrale.
The scientists hope to test the process in the next couple of years with the help of soldiers whose lungs have been damaged by chemicals and irritants they may have encountered in combat. The researchers will extend a light-emitting probe down into the soldiers’ lungs while the probe records images of the fluorescence in the surrounding tissues. They will then use HySP to create what amounts to a fluorescent map and compare it with that of healthy lung tissue to see if they can discern the damage. If so, they hope to further develop the technology so it may one day help these soldiers and other lung patients receive more targeted treatment.
It might also be possible one day for clinicians to use HySP to analyze cell phone pictures of skin lesions to determine if they are at risk of being cancerous, according to Fraser and Cutrale.
“We could determine if the lesions have changed color or shape over time,” Cutrale said. Clinicians could then examine the patient further to be certain of a diagnosis and respond appropriately.
Cutrale and Fraser see the technology as a giant leap forward for both research and medicine.
“Both scientists at the bench and scientists at the clinic will be able to perform their work faster and with greater confidence in the results,” Cutrale said. “Better, faster, cheaper. That’s the payoff here.”
Many infectious pathogens are difficult to treat because they develop into biofilms, layers of metabolically active but slowly growing bacteria embedded in a protective layer of slime, which are inherently more resistant to antibiotics. Now, a group of researchers at Caltech and the University of Oxford have made progress in the fight against biofilms.
The group identified a protein that degrades and inhibits biofilms of Pseudomonas aeruginosa, the primary pathogen in cystic fibrosis (CF) infections.
Aeruginosa enters a biofilm mode of growth in these contexts; biofilms tolerate conventional antibiotics much better than other modes of bacterial growth.
Pyocyanin has been used in the clinical identification of this strain for over a century, but several years ago the Newman group demonstrated that the molecule also supports biofilm growth, raising the possibility that its degradation might offer a new route to inhibit biofilm development.
“While there is precedent for the use of enzymes to treat bacterial infections, the novelty of this study lies in our observation that selectively degrading a small pigment that supports the biofilm lifestyle can inhibit biofilm expansion,” says Costa, the first author on the study.
While it will take several years of experimentation to determine whether the laboratory findings can be translated to a clinical context, the work has promise for the utilization of proteins like PodA to treat antibiotic-resistant biofilm infections, the researchers say.
Scientists persuade nature to make silicon-carbon bonds
A new study is the first to show that living organisms can be persuaded to make silicon-carbon bonds—something only chemists had done before. Scientists at Caltech “bred” a bacterial protein to have the ability to make the man-made bonds, a finding that has applications in several industries.
Molecules with silicon-carbon, or organosilicon, compounds are found in pharmaceuticals as well as in many other products, including agricultural chemicals, paints, semiconductors, and computer and TV screens. Currently, these products are made synthetically, since the silicon-carbon bonds are not found in nature.
The new research, which recently won Caltech’s Dow Sustainability Innovation Student Challenge Award (SISCA) grand prize, demonstrates that biology can instead be used to manufacture these bonds in ways that are more environmentally friendly and potentially much less expensive.
“We decided to get nature to do what only chemists could do—only better,” says Frances Arnold, Caltech’s Dick and Barbara Dickinson Professor of Chemical Engineering, Bioengineering and Biochemistry, and principal investigator of the new research, published in the Nov. 24 issue of the journal Science.
The study is also the first to show that nature can adapt to incorporate silicon into carbon-based molecules, the building blocks of life. Scientists have long wondered if life on Earth could have evolved to be based on silicon instead of carbon. Science-fiction authors likewise have imagined alien worlds with silicon-based life, like the lumpy Horta creatures portrayed in an episode of the 1960s TV series Star Trek. Carbon and silicon are chemically very similar. They both can form bonds to four atoms simultaneously, making them well suited to form the long chains of molecules found in life, such as proteins and DNA.
“No living organism is known to put silicon-carbon bonds together, even though silicon is so abundant, all around us, in rocks and all over the beach,” says Jennifer Kan, a postdoctoral scholar in Arnold’s lab and lead author of the new study. Silicon is the second most abundant element in Earth’s crust.
The researchers used a method called directed evolution, pioneered by Arnold in the early 1990s, in which new and better enzymes are created in labs by artificial selection, similar to the way that breeders modify corn, cows, or cats. Enzymes are a class of proteins that catalyze, or facilitate, chemical reactions. The directed evolution process begins with an enzyme that scientists want to enhance. The DNA coding for the enzyme is mutated in more-or-less random ways, and the resulting enzymes are tested for a desired trait. The top-performing enzyme is then mutated again, and the process is repeated until an enzyme that performs much better than the original is created.
Directed evolution has been used for years to make enzymes for household products, like detergents; and for “green” sustainable routes to making pharmaceuticals, agricultural chemicals, and fuels.
In the new study, the goal was not just to improve an enzyme’s biological function but to actually persuade it to do something that it had not done before. The researchers’ first step was to find a suitable candidate, an enzyme showing potential for making the silicon-carbon bonds.
“It’s like breeding a racehorse,” says Arnold, who is also the director of the Donna and Benjamin M. Rosen Bioengineering Center at Caltech. “A good breeder recognizes the inherent ability of a horse to become a racer and has to bring that out in successive generations. We just do it with proteins.”
The ideal candidate turned out to be a protein from a bacterium that grows in hot springs in Iceland. That protein, called cytochrome c, normally shuttles electrons to other proteins, but the researchers found that it also happens to act like an enzyme to create silicon-carbon bonds at low levels. The scientists then mutated the DNA coding for that protein within a region that specifies an iron-containing portion of the protein thought to be responsible for its silicon-carbon bond-forming activity. Next, they tested these mutant enzymes for their ability to make organosilicon compounds better than the original.
After only three rounds, they had created an enzyme that can selectively make silicon-carbon bonds 15 times more efficiently than the best catalyst invented by chemists. Furthermore, the enzyme is highly selective, which means that it makes fewer unwanted byproducts that have to be chemically separated out.
“This iron-based, genetically encoded catalyst is nontoxic, cheaper, and easier to modify compared to other catalysts used in chemical synthesis,” says Kan. “The new reaction can also be done at room temperature and in water.”
The synthetic process for making silicon-carbon bonds often uses precious metals and toxic solvents, and requires extra processing to remove unwanted byproducts, all of which add to the cost of making these compounds.
As to the question of whether life can evolve to use silicon on its own, Arnold says that is up to nature. “This study shows how quickly nature can adapt to new challenges,” she says. “The DNA-encoded catalytic machinery of the cell can rapidly learn to promote new chemical reactions when we provide new reagents and the appropriate incentive in the form of artificial selection. Nature could have done this herself if she cared to.”
Learn more: Bringing Silicon to Life
Findings have applications in novel therapeutics for cancer and other diseases
A new helper in the fight against cancer and other diseases of the gut may be genetically altered bacteria that release medicines to tumors or the gut.
Now, a new study performed using mice demonstrates how doctors might one day better regulate those therapeutic microbes by engineering them to respond to temperature. For instance, if engineered bacteria were administered to a patient with a disease, doctors could, in theory, instruct the bacteria to release medicine to just the site of interest, and nowhere else in the body, by using ultrasound to gently heat up the tissue.
“Bacteria can be designed to act like special agents fighting disease in our bodies,” says Caltech’s Mikhail Shapiro, assistant professor of chemical engineering and Heritage Principal Investigator, whose overall research goal is to create new ways to both visualize and control cells—bacterial cells and human cells—for medicinal purposes. “We’re building walkie-talkies for the cells so we can both listen and talk to them.”
Shapiro is principal investigator on a paper about the new research published November 14 in the journal Nature Chemical Biology. The colead authors are Dan Piraner and Mohamad Abedi, graduate students in Shapiro’s lab.
The research also shows how these engineered bacteria, once in a patient, could be programmed to stop administering a therapeutic or to self-destruct if the patient’s temperature rises from a fever. A fever might signal that the therapy is not working, and thus it would be in the patient’s best interest for the bacteria to terminate its activity.
In another application of the technology, the researchers demonstrated how the bacteria could be designed to destroy themselves once they leave a patient’s body through defecation. The lower temperature outside of a host’s body would signal the engineered bacteria to activate a genetic kill switch, thereby alleviating concerns about the genetically altered microbes spreading to the environment.
“We can use these thermal switches in bacteria to control a variety of behaviors,” says Shapiro.
The strategy of using engineered bacteria to fight disease—part of a growing field called microbial therapeutics—has shown some promise in animal models and humans. Previous research has demonstrated that some bacteria naturally make their way to tumor sites because they prefer the tumors’ low-oxygen environments. Studies have shown that these bacteria can be directed to release a medicine onto tumors, such as the tumor-destroying drug hemolysin. Other studies have shown that bacteria administered to the gut can release molecules to reduce inflammation. But these bacteria might end up in other portions of the body, and not just at the sites of interest.
The method developed by Shapiro’s lab solves this problem by providing a mechanism through which bacteria can be instructed to direct drugs only to a specific anatomical site. The idea is that the genetically engineered bacteria would activate their therapeutic program at a certain temperature induced via ultrasound tools, which gently heat tissues with millimeter precision. A doctor could, in theory, administer genetically altered bacteria to a cancer patient and then, by focusing ultrasound at the tumor site, trigger the bacteria to fight the tumor.
“We can spatially and temporally control the activity of the bacteria,” says Abedi. “We can communicate with them and tell them when and where something needs to be done.”
To create thermally controllable bacteria, the team first needed to find candidate genetic switches whose activity depends on temperature changes. They ultimately identified two candidates. The first is a protein in Salmonella bacteria, and the second originates from a bacterial virus called a bacteriophage. Both proteins bind to DNA to turn a genetic circuit on or off in response to temperature.
Next, the scientists used a protein engineering technique—”directed evolution,” pioneered by Caltech’s Frances Arnold—to evolve the proteins in the lab and tune their switching temperatures. For instance, the Salmonella protein was originally activated by temperatures ranging between 42 and 44 degrees Celsius. Using directed evolution, the scientists generated versions with activation temperatures between 36 and 39 degrees Celsius. When these genetic switches are used to control the expression of therapeutic proteins, they can act like thermal controls to turn the therapy on or off at a given temperature.
“When we were thinking about how to get bacteria to sense temperature, we looked at nature and found a few systems where bacteria can do this,” says Piraner. “We tested the performance, found the ones that had the best switching performance. From there, we went on to find that they could be tuned and amplified. It all started with what nature gave us, and engineering took us the rest of the way.”
Learn more: Biologists Give Bacteria Thermostat Controls
Berkeley Lab approach could lead to more stable, efficient artificial photosystems
Scientists have found a way to engineer the atomic-scale chemical properties of a water-splitting catalyst for integration with a solar cell, and the result is a big boost to the stability and efficiency of artificial photosynthesis.
Led by researchers at the Department of Energy’s Lawrence Berkeley National Laboratory (Berkeley Lab), the project is described in a paper published this week in the journal Nature Materials.
The research comes out of the Joint Center for Artificial Photosynthesis (JCAP), a DOE Energy Innovation Hub established in 2010 to develop a cost-effective method of turning sunlight, water, and carbon dioxide into fuel. JCAP is led by the California Institute of Technology with Berkeley Lab as a major partner.
The goal of this study was to strike a careful balance between the contradictory needs for efficient energy conversion and chemically sensitive electronic components to develop a viable system of artificial photosynthesis to generate clean fuel.
Striking the right balance
“In order for an artificial photosystem to be viable, we need to be able to make it once, deploy it, and have it last for 20 or more years without repairing it,” said study principal investigator Ian Sharp, head of materials integration and interface science research at JCAP.
The problem is that the active chemical environments needed for artificial photosynthesis are damaging to the semiconductors used to capture solar energy and power the device.
“Good protection layers are dense and chemically inactive. That is completely at odds with the characteristics of an efficient catalyst, which helps to split water to store the energy of light in chemical bonds,” said Sharp, who is also a staff scientist at Berkeley Lab’s Chemical Sciences Division. “The most efficient catalysts tend to be permeable and easily transform from one phase to another. These types of materials would usually be considered poor choices for protecting electronic components.”
By engineering an atomically precise film so that it can support chemical reactions without damaging sensitive semiconductors, the researchers managed to satisfy contradictory needs for artificial photosystems.
“This gets into the key aspects of our work,” said study lead author Jinhui Yang, who conducted the work as a postdoctoral researcher at JCAP. “We set out to turn the catalyst into a protective coating that balances these competing properties.”
Doing double duty
The researchers knew they needed a catalyst that could not only support active and efficient chemical reactions, but one that could also provide a stable interface with the semiconductor, allow the charge generated by the absorption of light from the semiconductor to be efficiently transferred to the sites doing catalysis, and permit as much light as possible to pass through.
They turned to a manufacturing technique called plasma-enhanced atomic layer deposition, performed at the Molecular Foundry at Berkeley Lab. This type of thin-film deposition is used in the semiconductor industry to manufacture integrated circuits.
“This technique gave us the level of precision we needed to create the composite film,” said Yang. “We were able to engineer a very thin layer to protect the sensitive semiconductor, then atomically join another active layer to carry out the catalytic reactions, all in a single process.”
The first layer of the film consisted of a nanocrystalline form of cobalt oxide that provided a stable, physically robust interface with the light-absorbing semiconductor. The other layer was a chemically reactive material made of cobalt dihydroxide.
“The design of this composite coating was inspired by recent advances in the field that have revealed how water-splitting reactions occur, at the atomic scale, on materials. In this way, mechanistic insights guide how to make systems that have the functional properties we need,” said Sharp.
Using this configuration, the researchers could run photosystems continuously for three days—potentially longer—when such systems would normally fail in mere seconds.
“A major impact of this work is to demonstrate the value of designing catalysts for integration with semiconductors,” said Yang. “Using a combination of spectroscopic and electrochemical methods, we showed that these films can be made compact and continuous at the nanometer scale, thus minimizing parasitic light absorption when integrated on top of photoactive semiconductors.”
The study authors noted that while this is an important milestone, there are many more steps needed before a commercially viable artificial photosystem is ready for deployment.
“In general, we need to know more about how these systems fail so we can identify areas to target for future improvement,” said Sharp. “Understanding degradation is an important avenue to making something that is stable for decades.”
Seeing deep into space requires large telescopes. The larger the telescope, the more light it collects, and the sharper the image it provides.
For example, NASA’s Kepler space observatory, with a mirror diameter of under one meter, is searching for exoplanets orbiting stars up to 3,000 light-years away. By contrast, the Hubble Space Telescope, with a 2.4-meter mirror, has studied stars more than 10 billion light-years away.
Now Caltech’s Sergio Pellegrino and colleagues are proposing a space observatory that would have a primary mirror with a diameter of 100 meters—40 times larger than Hubble’s. Space telescopes, which provide some of the clearest images of the universe, are typically limited in size due to the difficulty and expense of sending large items into space. Pellegrino’s team would circumvent that issue by shipping the mirror up as separate components that would be assembled, in space, by robots.
Their design calls for the use of more than 300 deployable truss modules that could be unfolded to form a scaffolding upon which a commensurate number of small mirror plates could be placed to create a large segmented mirror. The assembly of the scaffolding and the attachment of the many mirrors is a task well-suited to robots, Pellegrino and his colleagues say.
In their concept, a spider-like, six-armed “hexbot” would assemble the trusswork and then crawl across the structure to build the mirror atop it. It was modeled on the JPL RoboSimian system, which in 2015 completed the DARPA Robotics Challenge, a federal competition aimed at spurring the development of robots that could perform complicated tasks that would be dangerous for humans. The hexbot would run on electrical power from the telescope’s solar grid. It would use four of its arms to walk—with one leg moving at any given time, while the three others remain securely attached to the structure. The two remaining arms would be free to assemble the trusses and mirrors.
The team opted to pursue an ambitious 100-meter design. “We wanted to study how different kinds of architectures perform as the diameter is increased,” says Pellegrino, Joyce and Kent Kresa Professor of Aeronautics and Professor of Civil Engineering in Caltech’s Division of Engineering and Applied Science, and Jet Propulsion Laboratory Senior Research Scientist. “We found that far away from the Earth, a structurally connected telescope is much heavier than an architecture based on separate spacecraft for the primary mirror, the optics, and the instrumentation.”
The realization of such an assembly is still decades away. However, Pellegrino and his colleagues are already working on the various technologies that will be needed to make it possible.
The entire space observatory would be composed of the fully assembled mirror-and-truss structure and three other parts, flying in formation. An optics and instrumentation unit would be located about 400 meters from the mirror; a control unit, stationed about 400 meters beyond that, would align the system and keep it working properly; and a thin shade, roughly 20 meters in diameter, would shield the mirror from the sun to keep its temperature stable and consistent across its diameter.
The four-part assembly would be stationed at one of the sun–earth Lagrange points—locations between the sun and the earth where the pull of gravity from two bodies locks a satellite into orbit with them, allowing it to maintain a stable position. There, the space observatory could peer deep into space without drifting out of place.
Low-cost coating would disrupt the building retrofit market and potentially save billions in electricity
It’s estimated that 10 percent of all the energy used in buildings in the U.S. can be attributed to window performance, costing building owners about $50 billion annually, yet the high cost of replacing windows or retrofitting them with an energy efficient coating is a major deterrent. U.S. Dept. of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) researchers are seeking to address this problem with creative chemistry—a polymer heat-reflective coating that can be painted on at one-tenth the cost.
“Instead of hiring expensive contractors, a homeowner could go to the local hardware store, buy the coating, and paint it on as a DIY retrofit—that’s the vision,” said Berkeley Lab scientist Raymond Weitekamp. “The coating will selectively reflect the infrared solar energy back to the sky while allowing visible light to pass through, which will drastically improve the energy efficiency of windows, particularly in warm climates and southern climates, where a significant fraction of energy usage goes to air conditioning.”
A team of Berkeley Lab scientists is receiving part of a $3.95 million award from the Department of Energy’s Advanced Research Projects Agency–Energy (ARPA-E) to develop this product. The multi-institutional team is led by researcher Garret Miyake at the University of Colorado Boulder, and also includes Caltech and Materia Inc.
There are retrofit window films on the market now that have spectral selectivity, but a professional contractor is needed to install them, a barrier for many building owners. A low-cost option could significantly expand adoption and result in potential annual energy savings of 35 billion kilowatt-hours, reducing carbon dioxide emissions by 24 billion kilograms per year, the equivalent of taking 5 million cars off the road.
The Berkeley Lab technology relies on a type of material called a bottlebrush polymer, which, as its name suggests, has one main rigid chain of molecules with bristles coming off the sides. This unusual molecular architecture lends it some unique properties, one being that it doesn’t entangle easily.
“Imagine spaghetti versus gummy worms,” Weitekamp explained. “Spaghetti can be tied up in knots. If you want to rearrange cooked spaghetti back to its uncooked alignment, you would have to put significant energy into unwinding it. But with gummy worms you can line them all up easily because they’re pretty rigid.”
As a graduate student at Caltech, Weitekamp worked on understanding and controlling how bottlebrush polymers self-assemble into nanostructures behaving as photonic crystals, which can selectively reflect light at different frequencies. Last year he came to Berkeley Lab as part of Cyclotron Road, a program for entrepreneurial researchers, to commercialize these coatings and other related polymer-based technologies. He has been working on the development of polymeric materials as a user at the Molecular Foundry, a DOE Office of Science User Facility at Berkeley Lab.
“We were very compelled by the potential impact of [Weitekamp’s] technology across a number of industries,” said Cyclotron Road director Ilan Gur. “His ideas aligned with the Foundry’s expertise in polymer chemistry and the window application fit squarely into Berkeley Lab’s existing strengths in buildings technology and energy analysis.”
For the ARPA-E award, Weitekamp is collaborating with Berkeley Lab’s Steve Selkowitz, a leading expert on building science and window technologies, and Arman Shehabi, an expert in analyzing energy use of buildings, to develop a cost-competitive and scalable product. Their target cost is $1.50 per square foot, one-tenth the current market cost for commercially installed energy efficient retrofit window coatings.
“ARPA-E invests in high-risk, high-reward projects,” Shehabi said. “The high reward in this project isn’t in the performance improvement. It’s transformative in how windows could be retrofitted—it’s something you can do yourself. The market need is very large, and there’s nothing low-cost out there that meets that need.”
Mathematical equations can make Internet communication via computer, mobile phone or satellite many times faster and more secure than today.
Results with software developed by researchers from Aalborg University in collaboration with the US universities the Massachusetts Institute of Technology (MIT) and California Institute of Technology (Caltech) are attracting attention in the international technology media.
A new study uses a four minute long mobile video as an example. The method used by the Danish and US researchers in the study resulted in the video being downloaded five times faster than state of the art technology. The video also streamed without interruptions. In comparison, the original video got stuck 13 times along the way.