Sara Volz, 17, from Colorado Springs, Colo., joined the quest for practical alternatives to petroleum-based fuels in the seventh grade. Now a high school senior, she may have found an answer in the oily pond scum growing under her bed.
?I was trying to use guided evolution, so artificial selection, to isolate populations of algae cells with abnormally high oil content,? she told NBC News.
The result is a population of algae that produces so much oil, so efficiently, that it bagged the grand prize Tuesday night in the Intel Science Talent Search, an elite science fair. The prize comes with a $100,000 scholarship.
Algae biofuel has long fascinated the green energy community as a promising alternative to other biofuels, such as corn-based ethanol, that take a bite out of the world?s food budget. But a problem has been to get the plants to produce oil at scale cheaply enough to compete with petroleum-based fuel.
Other researchers have approached the problem by tweaking the algae genome or selecting the prime environmental conditions for algae growth. Volz?s approach, she said, is different and lower cost. It relies on an herbicide that kills algae cells with low levels of an enzyme crucial to making oil.
?The idea is, if you introduce this chemical, you kill everything with really low oil production,? she explained. ?What you are left with is a population of cells with very high oil production.?
Volz grew (and killed) the algae under her bed, where she has set up a home laboratory with flasks, microscopes, and everything else a young scientist needs. She developed her interest in algae biofuels in the ninth grade as a ?perfect fusion? of her passions in alternative energy and biochemistry.
The young scientist should find access to a bigger lab at the Massachusetts Institute of Technology, where she?ll enroll this fall. The prize money, she said, ?will cover a significant chunk of those expenses.?
John Roach is a contributing writer for NBC News. To learn more about him, check out his website.
Tiger Woods hits from the second hole fairway during the third round of the Cadillac Championship golf tournament on Sunday, March 10, 2013, in Doral, Fla. (AP Photo/Wilfredo Lee)
Tiger Woods hits from the second hole fairway during the third round of the Cadillac Championship golf tournament on Sunday, March 10, 2013, in Doral, Fla. (AP Photo/Wilfredo Lee)
Tiger Woods looks at his shot on the fourth green during the third round of the Cadillac Championship golf tournament on Sunday, March 10, 2013, in Doral, Fla. (AP Photo/Wilfredo Lee)
Graeme McDowell, of Northern Ireland, looks at his shot on the eighth green during the third round of the Cadillac Championship golf tournament on Sunday, March 10, 2013, in Doral, Fla. (AP Photo/Wilfredo Lee)
Steve Stricker follows his shot from a first hole bunker during the third round of the Cadillac Championship golf tournament on Sunday, March 10, 2013, in Doral, Fla. (AP Photo/Alan Diaz)
Sergio Garcia, of Spain, follows his shot from the second tee during the third round of the Cadillac Championship golf tournament on Sunday, March 10, 2013, in Doral, Fla. (AP Photo/Alan Diaz)
DORAL, Fla. (AP) ? Tiger Woods is hitting his stride on his march to the Masters.
Woods had full control of his game Sunday and never let anyone get closer than three shots until he had locked up his 17th World Golf Championship title. With a bogey that didn't matter on the final hole, he closed with a 1-under 71 to win the Cadillac Championship.
One year ago at Doral, Woods left after the 11th hole with tightness in his left Achilles tendon. He since has won five times in his last 22 tournaments worldwide, and can return to No. 1 in the world with a win in two weeks at Bay Hill.
Woods won by two over Steve Stricker, who gave Woods a putting tip on the eve of the tournament.
Tooele city fire investigators are working to determine the cause of fire that gutted the family room of a residence on Sunday.
The homeowner reported the blaze just after 5 p.m. The city?s volunteer fire department extinguished the fire within 45 minutes, Fire Chief Gary Coon said.
The family room and its contents were destroyed, but the home remains habitable, he said. An early estimate placed the damages at about $10,000.
The cause of the fire remained undetermined Sunday.
No one was injured, although the homeowner, who was home alone when the fire broke out, was treated at the scene for light smoke inhalation, Coon said.
jdobner@sltrib.com
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Contact: Michael Hottiger hottiger@vetbio.uzh.ch 41-446-355-474 University of Zurich
This press release is available in German.
Protein activity is strictly regulated. Incorrect or poor protein regulation can lead to uncontrolled growth and thus cancer or chronic inflammation. Members of the Institute of Veterinary Biochemistry and Molecular Biology from the University of Zurich have identified enzymes that can regulate the activity of medically important proteins. Their discovery enables these proteins to be manipulated very selectively, opening up new treatment methods for inflammations and cancer.
For a healthy organism, it is crucial for proteins to be active or inactive at the right time. The corresponding regulation is often based on a chemical modification of the protein structure: Enzymes attach small molecules to particular sites on a protein or remove them, thereby activating or deactivating the protein. Members of the Institute of Veterinary Biochemistry and Molecular Biology from the University of Zurich in collaboration with other Institutes have now discovered how the inactivation of a protein, which is important for medicine, can be reversed.
New group of ADP-ribosylhydrolases identified
An important protein modification is ADP-ribosylation, which is involved in certain types of breast cancer, cellular stress reactions and gene regulation. So-called ADP-ribosyltransferases attach the ADP ribose molecule to proteins, thereby altering their function. In recent years, many ADP-ribosyltransferases have been discovered that can convey single or several ADP-riboses to different proteins. Enzymes that can remove these riboses again, however, are less well known. Professor Michael Hottiger's team of researchers has now identified a new group of such ADP-ribosylhydrolases. The scientists discovered that a so-called macrodomain is responsible for removing the ADP-riboses in human proteins, but also in the bacterium Archaeoglobus fulgidus.
"We therefore assume that the reversal of the modification takes place in a similar way in different species," explains Michael Hottiger.
Biomedically relevant: inactivation of the modified enzyme GSK3?
The researchers also prove that ADP-ribosylhydrolases can remove the ADP-ribose of the intensively studied enzyme GSK3?, which regulates the synthesis of storage substances and is important in the progression of various diseases. ADP-ribosylation deactivates GSK3?, which can be reversed again by the newly identified enzyme. "Our discovery enables ADP-ribose modification to be manipulated and tested selectively, and new treatment methods developed for diseases such as inflammations or cancer," concludes Michael Hottiger.
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AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Contact: Michael Hottiger hottiger@vetbio.uzh.ch 41-446-355-474 University of Zurich
This press release is available in German.
Protein activity is strictly regulated. Incorrect or poor protein regulation can lead to uncontrolled growth and thus cancer or chronic inflammation. Members of the Institute of Veterinary Biochemistry and Molecular Biology from the University of Zurich have identified enzymes that can regulate the activity of medically important proteins. Their discovery enables these proteins to be manipulated very selectively, opening up new treatment methods for inflammations and cancer.
For a healthy organism, it is crucial for proteins to be active or inactive at the right time. The corresponding regulation is often based on a chemical modification of the protein structure: Enzymes attach small molecules to particular sites on a protein or remove them, thereby activating or deactivating the protein. Members of the Institute of Veterinary Biochemistry and Molecular Biology from the University of Zurich in collaboration with other Institutes have now discovered how the inactivation of a protein, which is important for medicine, can be reversed.
New group of ADP-ribosylhydrolases identified
An important protein modification is ADP-ribosylation, which is involved in certain types of breast cancer, cellular stress reactions and gene regulation. So-called ADP-ribosyltransferases attach the ADP ribose molecule to proteins, thereby altering their function. In recent years, many ADP-ribosyltransferases have been discovered that can convey single or several ADP-riboses to different proteins. Enzymes that can remove these riboses again, however, are less well known. Professor Michael Hottiger's team of researchers has now identified a new group of such ADP-ribosylhydrolases. The scientists discovered that a so-called macrodomain is responsible for removing the ADP-riboses in human proteins, but also in the bacterium Archaeoglobus fulgidus.
"We therefore assume that the reversal of the modification takes place in a similar way in different species," explains Michael Hottiger.
Biomedically relevant: inactivation of the modified enzyme GSK3?
The researchers also prove that ADP-ribosylhydrolases can remove the ADP-ribose of the intensively studied enzyme GSK3?, which regulates the synthesis of storage substances and is important in the progression of various diseases. ADP-ribosylation deactivates GSK3?, which can be reversed again by the newly identified enzyme. "Our discovery enables ADP-ribose modification to be manipulated and tested selectively, and new treatment methods developed for diseases such as inflammations or cancer," concludes Michael Hottiger.
###
[ | E-mail | Share ]
?
AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
As Community Radio for Northern Colorado, KUNC encourages the listing of all community events. Please utilize this free and easy-to-use service to promote your community activity here on the KUNC website. Please allow up to 48 hours for your event to appear on the KUNC website. Thank you!
In the last decade, we've seen tremendous changes in our workforce. With all of the recent advancement in technologies, nearly three-quarters of employers give their employees the tools they need to work remotely, giving employees more freedom to pick the hours they work.
Instead of designating the first hour of work to answer emails, the next hour to beating through phone calls, and the hours after to facilitating endless meetings due to protocol -- people now have the luxury of being able to complete their work at any point in time. But anyone who works remotely can tell you that even when the corporate structure is stripped away, being productive can still be a challenge.
"Telecommuting", as a recent article on Yahoo's decision to ban working beyond its walls calls it, has its fair share of disadvantages too. Ironically enough, in exchange for working remotely, most employees choose to work until later at night. Approximately 80 percent think it's okay to make a work-related call at night. As a result of these later hours, the work sometimes seeps into "off" hours, which can obviously take away time from your family and make it difficult to maintain a consistent social life.
With three million people working from home at least half the time, and 90 percent of them believing the flexibility of telecommuting improves their daily lives, it's no wonder people are looking for ways to become more productive at home.
How can you boost productivity so that you can maximize on your time? And at what point does all of this technology just get in the way of our work? 68 percent of women say technologies have not made them any more productive.
My newest blog in Fortune, "How to heal our smartphone-addled, overworked brains", answers this question. The biggest casualty of everyone being so connected is productivity. No one is getting much done at the office. In this blog, I go into the deeper science behind the "Healthy Mind Platter" that UCLA psychiatrist Dan Siegel and I launched in 2011. And this "platter" outlines seven types of mental activities the brain needs for optimal healthy functioning and I give a few tips you can maintain a healthy brain at work.
See more on the platter in the recent NeuroLeadership Journal.
See more on productivity in "How to heal our smartphone-addled, overworked brains".
The 2013 NeuroLeadership Summit is going local with three days of events in three different locations. Click here for more information.
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Follow David Rock on Twitter: www.twitter.com/davidrock101
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Public release date: 10-Mar-2013
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