Thursday, October 10, 2013

Thiel Fellows Program Is “Most Misdirected Piece Of Philanthropy,” Says Larry Summers

6258268010_14f0ff978c_bTwo years after billionaire tech investor Peter Thiel announced an experiment to pay bright high schoolers to drop out of college for $100,000, the Thiel Fellowship program hasn't won over education leaders.

"I think the single most misdirected bit of philanthropy in this decade is Peter Thiel's special program to drop out of college," said former Harvard President Larry Summers at the Nantucket Project conference during his first public appearance since removing himself for consideration for federal chairman.
Source: http://feedproxy.google.com/~r/Techcrunch/~3/9CRF1xAe_-M/
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Monday, August 5, 2013

Livermore makes breakthrough in solar energy research

The use of plasmonic black metals could someday provide a pathway to more efficient photovoltaics (PV) -- the use of solar panels containing photovoltaic solar cells -- to improve solar energy harvesting, according to researchers at Lawrence Livermore National Laboratory (LLNL).

The LLNL Materials Engineering Division (MED) research team has made breakthroughs experimenting with black metals. These nanostructured metals are designed to have low reflectivity and high absorption of visible and infrared light. The MED research team recently published their black metals research results in a cover-page article in the May issue of Applied Physics Letters titled "Plasmonic Black Metals in Resonant Nanocavities."

Authored by MED physicist and research team member Mihail Bora, the article details the work of the nanophotonics and plasmonics research team led by LLNL engineer Tiziana Bond.

It describes the team's concept of black metals, which are not classic metals but can be thought of as an extension of the black silicon concept. When silicon is treated in a certain way, such as being roughened at the nanoscale level, it traps light by multiple reflections, increasing its solar absorption. This gives the silicon a black surface that's able to better trap the full sun's wavelength spectrum.

Similarly, black metals are produced by some sort of random nanostructuring -- either in gold or silver -- without guaranteeing a full, reliable and repeatable full solar absorption.

However, Bond's team developed a method to improve and control the absorption efficiency and basically turn the metals as black as they want, allowing them to increase, on demand, the absorption of a higher quantity of solar wavelengths. Her team built nanopillar structures that are trapping and absorbing all the relevant wavelengths of the entire solar spectrum.

"Our article was picked for the cover story of Applied Physics Letters because it represents cutting-edge work in the area of plasmonics, the broadband operation obtained with a clear design and its implication for the photovoltaic yield," Bond said.

This new LLNL technology could one day be used in the energy harvesting industry such as PV. By incorporating metallic nanostructures with strong coupling of incident light, broad spectral and angular coverage, the LLNL team is providing a path for more efficient photovoltaics and thermovoltaics (a form of energy collection) by means of plasmon-exciton conversion, according to Bond and Bora.

Source: http://www.solardaily.com/reports/Lawrence_Livermore_engineering_team_makes_breakthrough_in_solar_energy_research_999.html

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Sunday, August 4, 2013

Powerball jackpot at $400M after no weekend winner

FILE- In this Nov. 28, 2012, file photo, Powerball numbers are chosen in the $579.9-million game drawing at the Florida Lottery in Tallahassee, Fla. No one hit the Powerball jackpot on Saturday, Aug. 3, 2013, so the $400-million prize will roll over for the next drawing on Wednesday. (AP Photo/Phil Sears, File)

FILE- In this Nov. 28, 2012, file photo, Powerball numbers are chosen in the $579.9-million game drawing at the Florida Lottery in Tallahassee, Fla. No one hit the Powerball jackpot on Saturday, Aug. 3, 2013, so the $400-million prize will roll over for the next drawing on Wednesday. (AP Photo/Phil Sears, File)

(AP) ? No one hit the Powerball jackpot this weekend, so the money will roll over and create a roughly $400 million prize for Wednesday's drawing.

The midweek jackpot remains below the record $590.5 million jackpot won in May by an 84-year-old Florida woman. But as it stands, it would be the third-largest Powerball jackpot ever and the fourth-largest lottery prize on record.

Saturday's winning numbers were 21, 24, 36, 42 and 45; the Powerball was 15.

The changes Powerball organizers made to the game last year are coming to roost in the billowing jackpots, with Wednesday's pushing into record territory less than three months after Gloria C. Mackenzie of Zephyrhills, Fla., claimed the biggest Powerball prize ever.

Powerball tickets doubled in price to $2 in January 2012 as part of a plan to help jackpots grow bigger, faster. And when the jackpots reach astronomical levels, ticket sales take off, with jackpots following close behind.

If Wednesday's jackpot doesn't top $400 million, a single winner choosing the cash option would collect $230.3 million before taxes.

No matter how many people play the game, the odds of matching all six numbers remains 1 in 175.2 million.

Half of the $2 cost of a Powerball ticket goes toward the prizes, the rest to the state lottery organization.

Powerball is played in 43 states, Washington, D.C., and the U.S. Virgin Islands.

Each state that participates in the game decides how to use the money. Some states earmark the money for a specific purpose, such as education, while others use it in their general funds.

___

Online:

www.powerball.com

Associated Press

Source: http://hosted2.ap.org/APDEFAULT/386c25518f464186bf7a2ac026580ce7/Article_2013-08-04-Powerball%20Jackpot/id-4c8e5f0f41724e5793b536db93e38442

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Wistar scientists decipher structure of NatA, an enzyme complex that modifies most human proteins

Wistar scientists decipher structure of NatA, an enzyme complex that modifies most human proteins [ Back to EurekAlert! ] Public release date: 4-Aug-2013
[ | E-mail | Share Share ]

Contact: Greg Lester
glester@wistar.org
215-898-3934
The Wistar Institute

Vital enzyme complex found elevated in many cancers

A team of researchers from Philadelphia and Norway has determined the structure of an enzyme complex that modifies one end of most human proteins and is made at elevated levels in numerous forms of cancer. A study in Nature Structural & Molecular Biology, led by researchers at The Wistar Institute, depicts the structure and the means of action of a protein complex called NatA. Their findings, they believe, will allow them to create an inhibitora potential drugthat could knock out NatA in order to curb the growth of cancer cells.

"NatA appears essential for the growth of cells and their ability to divide, and we can see elevated production of this enzyme in many forms of cancer" said Ronen Marmorstein, Ph.D., senior author, Hilary Koprowski, M.D. Professor, and leader of The Wistar Institute Cancer Center's Gene Expression and Regulation program. "Obviously, this is a particularly appealing drug target and we are currently leveraging our recent understanding of how the protein works to develop small molecules that will bind to and inactivate NatA."

NatA is a member of a family of N-terminal acetyltransferase (NAT) enzymes (or enzyme complexes) that modify proteins in order to control their behaviorfor example by turning proteins on, telling proteins where to move, and tagging proteins or the cell for destruction.

According to Marmorstein, NatA works with an amazing specificity for a particular sequence of amino acidsthe individual building blocks of proteinsand unraveling the roots of that specificity has proven an alluring puzzle for scientists.

The Marmorstein laboratory has proven expertise in the study of acetylation enzymes, proteins that modify other molecules in the cell with an acetyl group "tag." In the cellular world, structure dictates function, and acetylation is a universal process for controlling protein behavior and gene expression in living organisms.

"Modifying protein structures is one way that our cells control how proteins function," Marmorstein explained, "and enzymes in the NAT family modify nearly 85 percent of human proteins, and 50 percent of these are modified by NatA."

According to Marmorstein, NatA operates in a complex of two proteins, an enzymatic subunit and an auxiliary partner. When they developed the structure of NatAby bombarding a crystallized sample of the enzyme with powerful X-raysthey found how the auxiliary partner protein is crucial for turning the enzymatic subunit on.

Binding to an auxiliary protein causes a structural change in the enzymatic subunit that properly configures the active site of the proteinthe region of the protein where the chemical reaction occursessentially acting as a switch that activates the enzyme.

"When it binds to its auxiliary protein, the enzymatic subunit of NatA actually changes shape, reconfiguring the structure to allow it to properly grab its target protein N-terminal sequence for acetylation," Marmorstein said.

Importantly, others have found that NatA function is required for the proliferation of cancer cells. Marmorstein says, understanding the structure of NatA has allowed his team to better understand how to inactivate the protein in cancer cells. The structure has yielded targets for small molecules that will act as inhibitors, essentially stopping the protein by gumming up its structure.

###

The lead author of this study is Glen Liszczak, Ph.D., a graduate student working at the Wistar Institute from the University of Pennsylvania Department of Chemistry. Other co-authors of this study include, Jacob M. Goldberg, and E. James Petersson, Ph.D., from the University of Pennsylvania's Department of Chemistry; and Hrvard Foyn, Ph.D., and Thomas Arnesen, Ph.D., from the University of Bergen, Norway.

Funding for this project was through the National Institutes of Health grants GM060293 and GM071339. The Arnesen laboratory's efforts were supported by the Research Council of Norway and the Norwegian Cancer Society.


[ Back to EurekAlert! ] [ | E-mail | Share 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.


Wistar scientists decipher structure of NatA, an enzyme complex that modifies most human proteins [ Back to EurekAlert! ] Public release date: 4-Aug-2013
[ | E-mail | Share Share ]

Contact: Greg Lester
glester@wistar.org
215-898-3934
The Wistar Institute

Vital enzyme complex found elevated in many cancers

A team of researchers from Philadelphia and Norway has determined the structure of an enzyme complex that modifies one end of most human proteins and is made at elevated levels in numerous forms of cancer. A study in Nature Structural & Molecular Biology, led by researchers at The Wistar Institute, depicts the structure and the means of action of a protein complex called NatA. Their findings, they believe, will allow them to create an inhibitora potential drugthat could knock out NatA in order to curb the growth of cancer cells.

"NatA appears essential for the growth of cells and their ability to divide, and we can see elevated production of this enzyme in many forms of cancer" said Ronen Marmorstein, Ph.D., senior author, Hilary Koprowski, M.D. Professor, and leader of The Wistar Institute Cancer Center's Gene Expression and Regulation program. "Obviously, this is a particularly appealing drug target and we are currently leveraging our recent understanding of how the protein works to develop small molecules that will bind to and inactivate NatA."

NatA is a member of a family of N-terminal acetyltransferase (NAT) enzymes (or enzyme complexes) that modify proteins in order to control their behaviorfor example by turning proteins on, telling proteins where to move, and tagging proteins or the cell for destruction.

According to Marmorstein, NatA works with an amazing specificity for a particular sequence of amino acidsthe individual building blocks of proteinsand unraveling the roots of that specificity has proven an alluring puzzle for scientists.

The Marmorstein laboratory has proven expertise in the study of acetylation enzymes, proteins that modify other molecules in the cell with an acetyl group "tag." In the cellular world, structure dictates function, and acetylation is a universal process for controlling protein behavior and gene expression in living organisms.

"Modifying protein structures is one way that our cells control how proteins function," Marmorstein explained, "and enzymes in the NAT family modify nearly 85 percent of human proteins, and 50 percent of these are modified by NatA."

According to Marmorstein, NatA operates in a complex of two proteins, an enzymatic subunit and an auxiliary partner. When they developed the structure of NatAby bombarding a crystallized sample of the enzyme with powerful X-raysthey found how the auxiliary partner protein is crucial for turning the enzymatic subunit on.

Binding to an auxiliary protein causes a structural change in the enzymatic subunit that properly configures the active site of the proteinthe region of the protein where the chemical reaction occursessentially acting as a switch that activates the enzyme.

"When it binds to its auxiliary protein, the enzymatic subunit of NatA actually changes shape, reconfiguring the structure to allow it to properly grab its target protein N-terminal sequence for acetylation," Marmorstein said.

Importantly, others have found that NatA function is required for the proliferation of cancer cells. Marmorstein says, understanding the structure of NatA has allowed his team to better understand how to inactivate the protein in cancer cells. The structure has yielded targets for small molecules that will act as inhibitors, essentially stopping the protein by gumming up its structure.

###

The lead author of this study is Glen Liszczak, Ph.D., a graduate student working at the Wistar Institute from the University of Pennsylvania Department of Chemistry. Other co-authors of this study include, Jacob M. Goldberg, and E. James Petersson, Ph.D., from the University of Pennsylvania's Department of Chemistry; and Hrvard Foyn, Ph.D., and Thomas Arnesen, Ph.D., from the University of Bergen, Norway.

Funding for this project was through the National Institutes of Health grants GM060293 and GM071339. The Arnesen laboratory's efforts were supported by the Research Council of Norway and the Norwegian Cancer Society.


[ Back to EurekAlert! ] [ | E-mail | Share 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.


Source: http://www.eurekalert.org/pub_releases/2013-08/twi-wsd080213.php

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Obama tees off into birthday weekend with golf

WASHINGTON (AP) ? President Barack Obama kicked off his birthday weekend Saturday with a round of golf with friends and a getaway to Camp David.

Obama, who turns 52 on Sunday, left the White House just after 8 a.m. EDT ? that's unusually early for the half-hour motorcade ride to Andrews Air Force Base in Maryland ? to squeeze in some golf before the celebration shifted to the presidential retreat nestled in Maryland's Catoctin Mountains.

Before leaving, officials said Obama's counterterrorism adviser updated him on a potential al-Qaida threat that led the State Department on Friday to issue a global travel warning to Americans and order the weekend closure of 21 embassies and consulates across the Muslim world.

The White House said the president's three golfing foursomes included some of his friends from Hawaii, where he grew up, and Chicago, where he lived before becoming president, along with current and former aides.

Among them were childhood friends Bobby Titcomb and Mike Ramos, and Chicago pals Marty Nesbitt and Eric Whitaker. White House aides Marvin Nicholson and Sam Kass, an assistant chef, rounded out the group, along with Reggie Love, who for years had been Obama's personal assistant, or "body man," and basketball buddy until he left the White House in late 2011 to work on getting an MBA.

Due to the limited number of seats, only the winners at golf ? Love, Kass and two other players ? got to join Obama on the presidential helicopter. The losers went the long way, by car.

First lady Michelle Obama traveled to Camp David separately.

The White House said little about how Obama would celebrate on Saturday night and Sunday, but the birthday wishes started rolling in early.

House Democrats presented Obama with a birthday cake when he went up to the Capitol this week, and American Legion youth members sang "Happy Birthday" to him during a White House visit late last month.

For last year's birthday, which fell during his heated campaign for re-election, Obama also celebrated with a round of golf before heading to Camp David. But he later held several birthday-themed campaign fundraisers in Chicago, including one at his family's South Side home.

Obama is scheduled to return to the White House on Sunday.

___

Follow Darlene Superville on Twitter: http://www.twitter.com/dsupervilleap

Source: http://news.yahoo.com/obama-tees-off-birthday-weekend-golf-133841962.html

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Of particular concern to Consumers Union is the blurred distinction between "die...

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Saturday, August 3, 2013

Frankel Photography Offers Wedding, Bar Mitzvah Discounts Photo Packages

SAN MARCOS, CA, August 03, 2013 /24-7PressRelease/ -- Frankel Photography, a leading wedding, Bar Mitzvah, pet and family portrait photography studio in San Marcos, California, is having a huge summer sale on all wedding and Bar Mitzvah packages.

Through September 15, all Frankel Photography customers will receive a 10% discount on the package of their choice for Bar Mitzvah and wedding photo packages from this leading San Diego wedding photographer.

Owner and lead photographer at Frankel Photography, Albert Frankel has been in the photography business for more than three decades and knows that providing top quality customer service and professionalism go hand-in-hand when photographing a family's special occasion.

He said his studio is happy to offer discounted packages to two of the biggest special events possible. The summer sale on wedding and Bar Mitzvah packages at Frankel Photography will continue until September 15, 2013.

"We are happy to offer this discount on our top quality photography services for the summer months," said Frankel. "We know that these events can be very costly for a family so we'd like to make it a little easier for them use our professional photography services for their wedding or Bar Mitzvah."

Frankel also has enough experience in the photography business to know that using the most advanced equipment and lighting is the only way to deliver the very best photographic images to his clients. Recently, Frankel Photography starting using state of the art LED lighting in addition to traditional lighting methods when working on a photo shoot. "LED lighting give us much greater ability to create images that are guaranteed to amaze," said Frankel.

As lead photographer at Frankel Photography, Al Frankel brings an extensive portfolio of knowledge and experience to every event he covers. Frankel's uncanny camera sense and ability to capture the moment is evidenced in the warmth and style of his work. Heather Frankel is also a big part of the team, specializing in digital image processing and album design, her skills are essential in turning photographs into treasured memories.

About Frankel Photography: Frankel Photography, located in San Marcos, California, just outside San Diego, offers more than 27 years of experience as professional photographers specializing in wedding photography, Bar and Bat Mitzvah photography. The company offers expert special event photography, as well as pet photography and portrait photography.

For more information about Frankel Photography visit their website or call 760-402-2531.

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Press release service and press release distribution provided by http://www.24-7pressrelease.com

Source: http://finance.boston.com/boston/news/read?GUID=24802616

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