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Saturday, June 2, 2012

Sharethrough Launches A Video Portal To Show Off Ads That Don?t Suck

Ever want to re-watch one of those awesome and inspirational five-minute Nike ads, but didn't know where to look? Video ad distributor Sharethrough has rolled out a new video portal that is designed to bring together all the most innovative branded ads all in one place. With the launch of Sharethrough.tv, the startup hopes to aggregate the largest repository of branded videos on the web. By doing so, brands and agencies will be able to search through the most popular and most talked about ads produced over the last several years, all in one place. Users can search through the database to find specific ads, or they can browse through ads arranged by agency, brand, video type, or industry vertical.

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User:Home-based business opportunity 31-5-12 - UWMAV Wiki

From UWMAV Wiki

Who else is searching for Home-Based Business Opportunity?
With all the rise in technology specifically innovation in information technology during the last couple of years, fads of earning money are actually changing. Formerly, 9 to 5 jobs were much more common but together with the passage of time folks began acknowledging that it's pretty tough to remain outside the house for such a long time period. Due to this tough routine, most of the people particularly people who are married or are single mother or father started searching for those job opportunities which provide versatile timing so that they can also handle their household effortlessly. This gave rise to online jobs which may effortlessly be finished even though sitting down in the comfort of one's home. Aside from this, internet also supplies you home-based business opportunity. For sure, now you could start off and operate any business although sitting down at your house. Isn?t it fantastic?
You'll be able to conveniently get benefit from any home-based business opportunity but you should do history investigation prior to taking benefit from this opportunity. You may evaluate the expense and profits which you may get by getting advantage of any business enterprise opportunity. A big number of people are utilizing world-wide-web to perform part time positions for saving reasons while various other more confident and inspired men and women have began their own web based business enterprise and most of them are making money in 4 and 5 figures.
In relation to the home-based business opportunity provides by world-wide-web then you can find a huge number of options to think about. Even though, I cannot let you know about all these choices because it will probably be too time consuming but I might grant you some strategies and ideas for selecting the appropriate opportunity for yourself.
If you are significant about home-based business or work opportunities then you might turn out to be a supplier of any well-known company. There are no rigid guidelines for turning into a distributor of the well reputed company. In case you have very good communication skills and also you think that you may convince other individuals to but your merchandise then you may use this opportunity. These companies? provides you fixed amount of revenue on every single sale as finalized in your contract.
You could also act on farm to table concept as a sizable number of individuals are investing funds to begin a farm to table business nevertheless it surely demand substantial expenditure. A business following farm to table concept have a complete control over its suppliers and associates. It guarantees the quality of their items because they keep track of their suppliers as well as distributors.

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Friday, June 1, 2012

35 Action Photos That Will Give You Whiplash

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Houla massacre may have been 'crime against humanity': UN

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Let Springfield Bankruptcy Lawyers Guide You ? Gov Products

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Novel X-ray technique opens door to new biological insights

Public release date: 31-May-2012
[ | E-mail |

Share ]

Contact: Dr. Thomas Zoufal
presse@desy.de
49-408-998-1666
Helmholtz Association of German Research Centres

First high-resolution protein structure analysis demonstrates potential of free-electron lasers

This release is available in German.

Scientists have used a novel X-ray technique to peer into the internal structure of a common biomolecule. The study, published in the journal Science, demonstrates the immense potential of new tools called free-electron lasers to obtain high-resolution structural insight into macromolecules.

With the Linac Coherent Light Source (LCLS) at the U.S. SLAC National Accelerator Laboratory in California, the international team, including researchers from the Center for Free-Electron Laser Science (CFEL) at the campus of the German accelerator centre DESY in Hamburg, determined the structure of hen egg white lysozyme down to a resolution of 0.19 nanometres. Lysozyme was chosen as an already well-characterized model system to provide a proof-of-principle for the new technique. Despite the blazing intensity of the FEL X-ray pulses, which completely destroy the sample upon exposure, the method delivers high quality structural data, reports the team headed by SLAC scientist Sbastien Boutet.

"The exceptionally intense X-ray pulses possible with FELs open the door for analyzing completely new classes of biomolecules like proteins from the cell membrane, that are hard or nearly impossible to crystallize", explains co-author and CFEL scientist Henry Chapman of DESY: "This will allow us to explore uncharted terrain in structural biology." CFEL is a joint venture of DESY, the Max Planck Society and the University of Hamburg.

The structure of biomolecules is of great interest for medicine and biology, because their shape often determines their function. For example, when the structure of an enzyme critical to a cell receptor is known, it may be possible to design tailor-made medication. These structures are commonly determined by X-ray crystallography, in which crystallized samples are illuminated by an X-ray beam. The X-ray light is scattered by the regular arrangement of molecules in the crystal lattice and the resulting diffraction pattern allows the molecular structure to be calculated. However, the crystallization of many biomolecules is difficult and slow with a large failure rate.

Lysozyme is one of the best-characterized biomolecules, and its structure has been thoroughly investigated at conventional X-ray sources. For precisely this reason the team chose this protein as a known model system to demonstrate structural determination using an FEL to a resolution sufficiently high to see individual amino acids. The structure obtained from the FEL data matches well the known structure of lysozyme, obtained separately using much larger crystals. "The good agreement benchmarks the method, making it a valuable tool for systems that yield only tiny crystals," says co-author Ilme Schlichting from the Max Planck Institute for Medical Research in Heidelberg.

Novel X-ray lasers, such as the LCLS used in this study or the European XFEL currently being built in Hamburg, offer the possibility to study previously intractable molecular structures. The X-ray flashes from X-ray lasers are extremely bright so that only tiniest crystals are needed for a structure analysis. In fact, the micro crystals used in the study, measuring typically only 1 x 1 x 3 micrometres, almost immediately vaporize when subjected to the intense X-ray light. A flash from the LCLS is so short (only 5 million billionth of a second, or 5 femtoseconds) that it passes through the sample, carrying with it the information to form the diffraction pattern, all before the crystal has started to explode. "We were able to show that atomic resolution information can be collected before radiation damage has a chance to take effect," explains co-author and DESY scientist Anton Barty from the Chapman group. "The key is ultrashort pulses we see no effects of damage before the X-ray pulse has already passed."

The team previously demonstrated this new technique using different biomolecules. Prior to the published work in "Science", the obtained resolution was limited, however thanks to a new instrument at LCLS, the Boutet research team and collaborators were able for the first time to reach the resolution needed for detailed structural insight. The Coherent X-ray Imaging instrument (CXI) uses pulses of X-ray radiation with a wavelength of 0.132 nanometres generated by the LCLS (one nanometre is a millionth of a millimetre; visible light has wavelength between 400 and 800 nanometres).

Millions of small lysozyme crystals flowed through the laser beam in a liquid jet. From approximately 3.5 million X-ray flashes, the scientists registered about 100 000 hits, enabling the lysozyme structure to be determined with a resolution of 0.19 nanometres. "We're able to use the powerful pulses from LCLS to actually visualize the structure of the molecule at a resolution so high we start to infer the position of individual atoms," says Boutet. "This important demonstration shows that the technique works and it paves the way for a lot of exciting experiments to come."

###
About CFEL

The Center for Free-Electron Laser Science (CFEL) on the DESY campus Hamburg-Bahrenfeld is a joint enterprise of Deutsches Elektronen-Synchrotron DESY, the Max Planck Society and the University of Hamburg. CFEL is designed to advance science with so-called free-electron lasers (FELs). These novel light sources based on linear particle accelerators enable to observe nature live on the scale of single molecules and atoms. Leading scientists of various disciplines meet under the CFEL roof to work jointly on interdisciplinary themes. Currently, more than 140 CFEL colleagues form five divisions and two Advanced Study Groups. http://www.cfel.de/index_eng.html
About LCLS

The Linac Coherent Light Source is a U.S. Department of Energy Office of Science-funded facility located at the SLAC National Accelerator Laboratory. LCLS is the world's first hard X-ray free-electron laser, allowing researchers to see atomic-scale detail on ultrafast timescales. The LCLS enables groundbreaking research in physics, chemistry, structural biology, energy science and many other diverse fields. http://lcls.slac.stanford.edu
Original publication

"High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography"; Sbastien Boutet et al.; Science, DOI: 10.1126/science.1217737

[ | 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.

Novel X-ray technique opens door to new biological insights Public release date: 31-May-2012
[ | E-mail | Share ]
Contact: Dr. Thomas Zoufal
presse@desy.de
49-408-998-1666
Helmholtz Association of German Research Centres

First high-resolution protein structure analysis demonstrates potential of free-electron lasers

This release is available in German.

Scientists have used a novel X-ray technique to peer into the internal structure of a common biomolecule. The study, published in the journal Science, demonstrates the immense potential of new tools called free-electron lasers to obtain high-resolution structural insight into macromolecules.

With the Linac Coherent Light Source (LCLS) at the U.S. SLAC National Accelerator Laboratory in California, the international team, including researchers from the Center for Free-Electron Laser Science (CFEL) at the campus of the German accelerator centre DESY in Hamburg, determined the structure of hen egg white lysozyme down to a resolution of 0.19 nanometres. Lysozyme was chosen as an already well-characterized model system to provide a proof-of-principle for the new technique. Despite the blazing intensity of the FEL X-ray pulses, which completely destroy the sample upon exposure, the method delivers high quality structural data, reports the team headed by SLAC scientist Sbastien Boutet.

"The exceptionally intense X-ray pulses possible with FELs open the door for analyzing completely new classes of biomolecules like proteins from the cell membrane, that are hard or nearly impossible to crystallize", explains co-author and CFEL scientist Henry Chapman of DESY: "This will allow us to explore uncharted terrain in structural biology." CFEL is a joint venture of DESY, the Max Planck Society and the University of Hamburg.

The structure of biomolecules is of great interest for medicine and biology, because their shape often determines their function. For example, when the structure of an enzyme critical to a cell receptor is known, it may be possible to design tailor-made medication. These structures are commonly determined by X-ray crystallography, in which crystallized samples are illuminated by an X-ray beam. The X-ray light is scattered by the regular arrangement of molecules in the crystal lattice and the resulting diffraction pattern allows the molecular structure to be calculated. However, the crystallization of many biomolecules is difficult and slow with a large failure rate.

Lysozyme is one of the best-characterized biomolecules, and its structure has been thoroughly investigated at conventional X-ray sources. For precisely this reason the team chose this protein as a known model system to demonstrate structural determination using an FEL to a resolution sufficiently high to see individual amino acids. The structure obtained from the FEL data matches well the known structure of lysozyme, obtained separately using much larger crystals. "The good agreement benchmarks the method, making it a valuable tool for systems that yield only tiny crystals," says co-author Ilme Schlichting from the Max Planck Institute for Medical Research in Heidelberg.

Novel X-ray lasers, such as the LCLS used in this study or the European XFEL currently being built in Hamburg, offer the possibility to study previously intractable molecular structures. The X-ray flashes from X-ray lasers are extremely bright so that only tiniest crystals are needed for a structure analysis. In fact, the micro crystals used in the study, measuring typically only 1 x 1 x 3 micrometres, almost immediately vaporize when subjected to the intense X-ray light. A flash from the LCLS is so short (only 5 million billionth of a second, or 5 femtoseconds) that it passes through the sample, carrying with it the information to form the diffraction pattern, all before the crystal has started to explode. "We were able to show that atomic resolution information can be collected before radiation damage has a chance to take effect," explains co-author and DESY scientist Anton Barty from the Chapman group. "The key is ultrashort pulses we see no effects of damage before the X-ray pulse has already passed."

The team previously demonstrated this new technique using different biomolecules. Prior to the published work in "Science", the obtained resolution was limited, however thanks to a new instrument at LCLS, the Boutet research team and collaborators were able for the first time to reach the resolution needed for detailed structural insight. The Coherent X-ray Imaging instrument (CXI) uses pulses of X-ray radiation with a wavelength of 0.132 nanometres generated by the LCLS (one nanometre is a millionth of a millimetre; visible light has wavelength between 400 and 800 nanometres).

Millions of small lysozyme crystals flowed through the laser beam in a liquid jet. From approximately 3.5 million X-ray flashes, the scientists registered about 100 000 hits, enabling the lysozyme structure to be determined with a resolution of 0.19 nanometres. "We're able to use the powerful pulses from LCLS to actually visualize the structure of the molecule at a resolution so high we start to infer the position of individual atoms," says Boutet. "This important demonstration shows that the technique works and it paves the way for a lot of exciting experiments to come."

###
About CFEL

The Center for Free-Electron Laser Science (CFEL) on the DESY campus Hamburg-Bahrenfeld is a joint enterprise of Deutsches Elektronen-Synchrotron DESY, the Max Planck Society and the University of Hamburg. CFEL is designed to advance science with so-called free-electron lasers (FELs). These novel light sources based on linear particle accelerators enable to observe nature live on the scale of single molecules and atoms. Leading scientists of various disciplines meet under the CFEL roof to work jointly on interdisciplinary themes. Currently, more than 140 CFEL colleagues form five divisions and two Advanced Study Groups. http://www.cfel.de/index_eng.html
About LCLS

The Linac Coherent Light Source is a U.S. Department of Energy Office of Science-funded facility located at the SLAC National Accelerator Laboratory. LCLS is the world's first hard X-ray free-electron laser, allowing researchers to see atomic-scale detail on ultrafast timescales. The LCLS enables groundbreaking research in physics, chemistry, structural biology, energy science and many other diverse fields. http://lcls.slac.stanford.edu
Original publication

"High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography"; Sbastien Boutet et al.; Science, DOI: 10.1126/science.1217737

[ | 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.

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NYC proposes ban on large sodas at restaurants

Various size cups and sugar cubes are displayed at a news conference at New York's City Hall, Thursday, May 31, 2012. New York Mayor Michael Bloomberg is proposing a ban on the sale of large sodas and other sugary drinks in the city's restaurants, delis and movie theaters in the hopes of combating obesity, an expansion of his administration's efforts to encourage healthy behavior by limiting residents' choices. (AP Photo/Richard Drew)

Various size cups and sugar cubes are displayed at a news conference at New York's City Hall, Thursday, May 31, 2012. New York Mayor Michael Bloomberg is proposing a ban on the sale of large sodas and other sugary drinks in the city's restaurants, delis and movie theaters in the hopes of combating obesity, an expansion of his administration's efforts to encourage healthy behavior by limiting residents' choices. (AP Photo/Richard Drew)

A man leaves a 7-Eleven store with a Double Gulp drink, in New York, Thursday, May 31, 2012. New York Mayor Michael Bloomberg is proposing a ban on the sale of large sodas and other sugary drinks in the city's restaurants, delis and movie theaters in the hopes of combating obesity, an expansion of his administration's efforts to encourage healthy behavior by limiting residents' choices. (AP Photo/Richard Drew)

New York City Health Commissioner Thomas Farley, accompanied by Deputy Mayor for Health and Human Services Linda Gibbs, addresses a news conference at New York's City Hall, Thursday, May 31, 2012. New York Mayor Michael Bloomberg is proposing a ban on the sale of large sodas and other sugary drinks in the city's restaurants, delis and movie theaters in the hopes of combating obesity, an expansion of his administration's efforts to encourage healthy behavior by limiting residents' choices. (AP Photo/Richard Drew)

NEW YORK (AP) ? Want to super-size that soda? Sorry, but in New York City you could be out of luck.
In his latest effort to fight obesity in this era of Big Gulps and triple bacon cheeseburgers, Mayor Michael Bloomberg is proposing an unprecedented ban on large servings of soda and other sugary drinks at restaurants, delis, sports arenas and movie theaters.
Drinks would be limited to 16 ounces, which is considered a small at many fast-food joints.
"The percentage of the population that is obese is skyrocketing," Bloomberg said Thursday on MSNBC. He added: "We've got to do something."
It is the first time an American city has directly attempted to limit soda portion sizes, and opponents again accused the three-term mayor of creating a "nanny state" and robbing New Yorkers of the right to choose for themselves.
But city officials said they believe the plan ? expected to win approval from the Bloomberg-appointed Board of Health and take effect as soon as March ? will ultimately prove popular and push governments around the U.S. to adopt similar rules.
"We have a crisis of obesity," said city Health Commissioner Thomas Farley. "People often go with the default choice, and if the default choice is something which is very unhealthy and is feeding into that health crisis, it's appropriate for the government to say, 'No, we think the default choice should be healthier.'"
The soft drink industry responded with scathing criticism, even as the administration said it felt certain the companies could simply trim back their offerings from 20-ounce bottles to 16-ounce bottles ? reversing a trend that has been under way for decades. In the 1950s, McDonald's offered only one size for soft drinks: 7 ounces, city officials said.
Coca-Cola called the ban an "arbitrary mandate."
"The people of New York City are much smarter than the New York City Health Department believes," the company said in a statement. "New Yorkers expect and deserve better than this. They can make their own choices about the beverages they purchase."
The ban would apply only to sweetened drinks over 16 ounces that contain more than 25 calories per 8 ounces. (A 12-ounce can of Coke has about 140 calories.) It would not affect diet soda or any drink that is at least half milk or milk substitute.
Nor would it apply to drinks sold in supermarkets or convenience stores, unless those businesses primarily sell foods meant to be eaten right away. Businesses would face fines of $200 per failed inspection.
City officials said some calorie-heavy drinks such as Starbucks Frappuccinos would probably be exempted because of their dairy content, while the Slurpees at 7-Eleven wouldn't be affected because the stores are regulated as groceries.
Bloomberg said people who want to guzzle more than 16 ounces would still be free to order more than one drink. But he said restricting sodas to 16 ounces each could still help curb consumption.
"You tend to eat all of the food in the container. If it's bigger, you eat more. If somebody put a smaller glass or plate or bowl in front of you, you would eat less," he said.
In announcing the proposal, health officials cited research linking sugary drinks to rising rates of obesity, diabetes and heart disease.
"Sugar drinks are not the entire obesity epidemic, but they are uniquely, strongly associated with this rise in obesity over the last 30 years," Farley said. "There's something about sugar water, as a product, which leads to long-term weight gain."
At a Burger King in Manhattan, retired postal worker Bobby Brown didn't like the mayor's idea, saying people should be "free to choose what they drink or eat."
But Joseph Alan, a chauffeur eating at a nearby Subway, said his overweight friends' eating habits ultimately affect him, too: "I tell them, 'This is affecting our insurance, because charges go up more treating people with diabetes and other health problems. I don't want to pay more for health insurance so people have these drinks!'"
Under Bloomberg, New York has campaigned aggressively against obesity, outlawing trans fats in french fries and other restaurant food and forcing chain restaurants to list calories on menus. The mayor has also led efforts to ban smoking in the city's bars, restaurants, parks and beaches.
His administration has tried other ways to discourage soda consumption. The mayor supported a state tax on sodas, but the measure died in the Legislature, and he tried to restrict the use of food stamps to buy soda, an idea federal regulators rejected.
Mark Kalinowski, an analyst with Janney Capital Markets who covers companies including McDonald's, said it is unlikely the ban will be enacted. "Folks who want to buy Big Gulps and Frappuccinos, a lot of those customers, you're only going to be able to take it away from them by prying it out of their cold, dead hands," he said.
And if it does go into effect, he said, customers will probably just respond by ordering two drinks.
"Maybe the mayor can outlaw all soft drinks and outlaw all fun while he's at it," Kalinowski scoffed.
___
Follow Samantha Gross at www.twitter.com/samanthagross
___
AP Food Industry Writer Candice Choi and writers Karen Matthews and Verena Dobnik contributed to this report.
Associated Press
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