The U.S. Secret Service is investigating whether a shooting incident in Washington on Friday night was a rash attempt to fire at the White House.
The Secret Service disclosed Wednesday that investigators have recovered two bullet rounds that struck the White House ? one a window and the other the building's exterior.
The rounds may have been fired during a shooting on Friday night near the White House, but the two incidents have not been conclusively connected. Police are intensifying their search for a suspect in the first incident.
Initial police reports said the Friday shooting at around 9 p.m. involved two cars speeding along Constitution Avenue, the wide street south of the White House and the Ellipse. The shots were believed to have been fired from a moving car as it passed along the 1600 block, a little over a third of a mile from the White House, in an area between the White House and the Washington Monument.
No one was hurt. President Barack Obama and his wife Michelle were out of town on Friday night. The president was attending a basketball game in San Diego, before heading to Hawaii, where he hosted a weekend APEC summit of Asia-Pacific regional leaders.
Only on msnbc.com
Updated 48 minutes ago
11/16/2011 4:23:16 PM +00:00
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The car from which U.S. Park Service police believe the shots were fired was found about seven blocks away, crashed into a barrier, with an assault-type rifle still inside. About 10 shell casings were also found in the car, indicating that the shots were fired from inside the vehicle, NBC News reported.
The car has been traced to Oscar Ramiro Ortega, 21, who has connections to Idaho, Utah, and Texas, authorities said. He is also known by the name Oscar Ramiro Ortega-Hernandez, according to the Secret Service.
A warrant was issued for his arrest, on a charge of carrying a dangerous weapon. It's illegal to possess or discharge a firearm in the District of Columbia.
Ortega remains at large.
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Now, investigators are looking into whether he was shooting at the White House, and they're now working to determine whether the two rounds found Tuesday came from the weapon that was in his car.
"Damage to an exterior window was discovered at the White House. A round was stopped by ballistic glass behind the historic exterior glass. One additional round has been found on the exterior of the White House," Secret Service officials said.
Nearly all the windows in the White House have bullet-resistant glass behind the original historic windows, and it is a robust building.
Story: Police probe gunfire reported near White House
"Specifically what he was aiming at, or not aiming at, is something that would be better addressed by interviewing him," U.S. Park Police spokesman Sgt. David Schlosser said, according to The Washington Post. "Otherwise, it's just speculation."
Ortega has a criminal record including arrests for domestic violence, drug offenses, assault on a police officer and underage alcohol possession, the Post reported.
Law enforcement has searched for him in the Occupy DC camp at McPherson Square, NBC Washington reported. Park police believe Ortega came to the D.C. area several weeks ago and may still be in the area, the station reported.
Investigators say Ortega has several distinctive tattoos, including several dots on his right hand. He also has the word "Israel" tattooed on the left side of his neck. U.S. Park Police say he also has several other tattoos on his chest and back including the name "Ortega," hands clasped in prayer and rosary beads.
ABC News reported that police believe the suspect is mentally ill. Sources told ABC that investigators have uncovered evidence suggesting he has a fixation on the White House.
NBC's Pete Williams and Brian Mooar, NBC Washington, The Associated Press and msnbc.com staff contributed to this report.
Yes. In the social hierarchy of prison inmates, mob kingpins, accomplished bank robbers, and cop killers tend to get the most respect. Convicts who have committed crimes against children, especially sexual abuse, are hated, harassed, and abused. Many inmates refer to molesters as ?dirty? prisoners, and some insist that assaulting or killing them represents a service to society. But a convict?s crime plays only a small role in his social status and safety. Most jailhouse assaults happen because the victim violated prison norms, not because of the crime he committed on the outside. Those who steal tobacco, disrespect the members of an opposing gang, or snitch are in for a much rougher ride than the average molester.
Creation of the largest human-designed protein boosts protein engineering effortsPublic release date: 15-Nov-2011 [ | E-mail | Share ]
Contact: David F. Salisbury david.salisbury@vanderbilt.edu 615-343-6803 Vanderbilt University
If Guinness World Records had a category for the largest human-designed protein, then a team of Vanderbilt chemists would have just claimed it.
They have designed and successfully synthesized a variant of a protein that nature uses to manufacture the essential amino acid histidine. It is more than twice the size of the previous record holder, a protein created by researchers at the University of Washington in 2003.
The synthetic protein, designated FLR, validates a new approach which the Vanderbilt scientists have developed that allows them to design functional artificial proteins substantially larger than previously possible.
"We now have the algorithms we need to engineer large proteins with shapes that you don't see in nature. This gives us the tools we need to create new, more effective antibodies and other beneficial proteins," said Jens Meiler, the associate professor of chemistry at Vanderbilt who led the effort.
Recently, protein engineers have verified a potential treatment strategy for HIV by using designed protein vaccines in mice and have designed artificial proteins that mimic antibodies in broadly neutralizing flu infections. The technique developed at Vanderbilt promises to expand the scope of these efforts substantially.
That is important because proteins are the most important molecules in living cells. They perform most of the vital tasks that take place within a living organism. There are hundreds of thousands of different proteins. They come in a variety of shapes and sizes. They can be round or long and thin, rigid or flexible. But they are all made out of linear chains of 20 amino acids encoded in the genome of the organism.
Proteins assume this variety of shapes and sizes by the manner in which they bunch and fold. This complex process takes two steps. First, small numbers of adjacent amino acids form what scientists call secondary structures: the most common of which are a rod-like spiral shape called the alpha-helix and a flat, pleated shape called the beta-sheet. These secondary structures, in turn, interact, fold and coil to form the protein's three-dimensional shape, which is the key to its function.
Over the past 10 years an increasing number of proteins that don't exist in nature have been designed "in silico" (in a computer). Scientists use sophisticated protein modeling software that incorporates the relevant laws of physics and chemistry to find amino acid sequences that fold into stable forms and have specific functions.
Imagine making a necklace 10 beads long with beads that come in 20 different colors. There are more than 10 trillion different combinations to choose among. This provides an idea of the complexity involved in designing novel proteins. For a protein of a given size, the modeling software creates millions of versions by putting each amino acid in every position and evaluating the stability of the resulting molecule. This takes a tremendous amount of computing power which skyrockets as the length of the protein increases.
"The current limit of this approach, even using the fastest supercomputers, is about 120 amino acids," said Meiler. The previous record holder contained 106 amino acids. The newly designed protein contains 242 amino acids. The Vanderbilt group got around this limit by modifying the widely used protein engineering platform called ROSETTA so that it can incorporate symmetry in the design process.
Their success provides new support for a controversial theory about protein evolution called the gene duplication and fusion hypothesis. The advantage of small proteins is that they can evolve rapidly in response to changing conditions, but larger proteins can perform more complex functions. Nature found a way to get both advantages by selecting small proteins that can interact with other copies of themselves to form larger proteins, which are called dimers. Once useful dimers have been created the gene that coded for the original protein is duplicated and fused to form a new gene that can directly produce the dimer. After it is created, the dimer gene is gradually modified by natural selection to make it more efficient or develop new functions.
Because they have two identical halves, dimers have a large degree of symmetry. By taking these symmetries into account, the Vanderbilt group was able to substantially reduce the amount of computing time required to create the FLR protein. Using 400 processors of the supercomputer at Vanderbilt's Advanced Computing Center for Research and Education, it took 10 days of continuous processing to find the most stable configuration.
To check the accuracy of their design, the researchers synthesized the DNA sequence that produces the protein, inserted it in E.coli bacteria and determined that they produced the protein and it folded properly.
The FLR protein assumes a 3-D shape called a TIM barrel, which is found in 10 percent of proteins and is particularly prevalent among enzymes. It is formed from eight beta strands that are surrounded by eight alpha helices arranged in a hexagonal shape like a tiny barrel.
###
The paper reporting this achievement appears in the Nov. 16 issue of the Journal of American Chemical Society and is available online. Members of Meiler's team are research assistant Carie Fortenberry, undergraduate students Elizabeth Bowman, Will Proffitt, and Brent Dorr and research assistant professors of biochemistry Joel Harp and Laura Mizoue. The research was supported by grants from the Defense Advanced Research Projects Agency's protein design project and the National Science Foundation.
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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.
Creation of the largest human-designed protein boosts protein engineering effortsPublic release date: 15-Nov-2011 [ | E-mail | Share ]
Contact: David F. Salisbury david.salisbury@vanderbilt.edu 615-343-6803 Vanderbilt University
If Guinness World Records had a category for the largest human-designed protein, then a team of Vanderbilt chemists would have just claimed it.
They have designed and successfully synthesized a variant of a protein that nature uses to manufacture the essential amino acid histidine. It is more than twice the size of the previous record holder, a protein created by researchers at the University of Washington in 2003.
The synthetic protein, designated FLR, validates a new approach which the Vanderbilt scientists have developed that allows them to design functional artificial proteins substantially larger than previously possible.
"We now have the algorithms we need to engineer large proteins with shapes that you don't see in nature. This gives us the tools we need to create new, more effective antibodies and other beneficial proteins," said Jens Meiler, the associate professor of chemistry at Vanderbilt who led the effort.
Recently, protein engineers have verified a potential treatment strategy for HIV by using designed protein vaccines in mice and have designed artificial proteins that mimic antibodies in broadly neutralizing flu infections. The technique developed at Vanderbilt promises to expand the scope of these efforts substantially.
That is important because proteins are the most important molecules in living cells. They perform most of the vital tasks that take place within a living organism. There are hundreds of thousands of different proteins. They come in a variety of shapes and sizes. They can be round or long and thin, rigid or flexible. But they are all made out of linear chains of 20 amino acids encoded in the genome of the organism.
Proteins assume this variety of shapes and sizes by the manner in which they bunch and fold. This complex process takes two steps. First, small numbers of adjacent amino acids form what scientists call secondary structures: the most common of which are a rod-like spiral shape called the alpha-helix and a flat, pleated shape called the beta-sheet. These secondary structures, in turn, interact, fold and coil to form the protein's three-dimensional shape, which is the key to its function.
Over the past 10 years an increasing number of proteins that don't exist in nature have been designed "in silico" (in a computer). Scientists use sophisticated protein modeling software that incorporates the relevant laws of physics and chemistry to find amino acid sequences that fold into stable forms and have specific functions.
Imagine making a necklace 10 beads long with beads that come in 20 different colors. There are more than 10 trillion different combinations to choose among. This provides an idea of the complexity involved in designing novel proteins. For a protein of a given size, the modeling software creates millions of versions by putting each amino acid in every position and evaluating the stability of the resulting molecule. This takes a tremendous amount of computing power which skyrockets as the length of the protein increases.
"The current limit of this approach, even using the fastest supercomputers, is about 120 amino acids," said Meiler. The previous record holder contained 106 amino acids. The newly designed protein contains 242 amino acids. The Vanderbilt group got around this limit by modifying the widely used protein engineering platform called ROSETTA so that it can incorporate symmetry in the design process.
Their success provides new support for a controversial theory about protein evolution called the gene duplication and fusion hypothesis. The advantage of small proteins is that they can evolve rapidly in response to changing conditions, but larger proteins can perform more complex functions. Nature found a way to get both advantages by selecting small proteins that can interact with other copies of themselves to form larger proteins, which are called dimers. Once useful dimers have been created the gene that coded for the original protein is duplicated and fused to form a new gene that can directly produce the dimer. After it is created, the dimer gene is gradually modified by natural selection to make it more efficient or develop new functions.
Because they have two identical halves, dimers have a large degree of symmetry. By taking these symmetries into account, the Vanderbilt group was able to substantially reduce the amount of computing time required to create the FLR protein. Using 400 processors of the supercomputer at Vanderbilt's Advanced Computing Center for Research and Education, it took 10 days of continuous processing to find the most stable configuration.
To check the accuracy of their design, the researchers synthesized the DNA sequence that produces the protein, inserted it in E.coli bacteria and determined that they produced the protein and it folded properly.
The FLR protein assumes a 3-D shape called a TIM barrel, which is found in 10 percent of proteins and is particularly prevalent among enzymes. It is formed from eight beta strands that are surrounded by eight alpha helices arranged in a hexagonal shape like a tiny barrel.
###
The paper reporting this achievement appears in the Nov. 16 issue of the Journal of American Chemical Society and is available online. Members of Meiler's team are research assistant Carie Fortenberry, undergraduate students Elizabeth Bowman, Will Proffitt, and Brent Dorr and research assistant professors of biochemistry Joel Harp and Laura Mizoue. The research was supported by grants from the Defense Advanced Research Projects Agency's protein design project and the National Science Foundation.
[ | 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.
Wages are increasing a lot faster in China than in the US. Some are saying that's a good thing, because it will keep jobs in the US, but the problem is that productivity is going up a lot faster in China as well.
Perennial optimist Mark Perry tries to spin the news that wages are increasing a lot faster in China than in the U.S. as something positive for the U.S. because this will lead to more manufacturing staying in the U.S.
Skip to next paragraph Stefan Karlsson
Stefan is an economist currently working in Sweden.
Recent posts
He is right in the sense that all else being equal lower relative wages in the U.S. will increase the willingness of companies to invest in the U.S. rather than China. However, though lower wages is a potential mean by which to increase employment, it is negative as a self-end. That is especially true to the extent it reflects lower relative productivity, because to the extent to which productivity is also lower it will not increase employment.
This can be illustrated by the fact that average hourly earnings is more than twice as high in Germany than in Greece, but as should be obvious especially these days, that doesn't mean that Greece is more competitive than Germany, because German productivity exceeds Greek productivity even more. And though wages are increasing a lot faster in China than in the U.S., so is productivity.
The Christian Science Monitor has assembled a diverse group of the best economy-related bloggers out there. Our guest bloggers are not employed or directed by the Monitor and the views expressed are the bloggers' own, as is responsibility for the content of their blogs. To contact us about a blogger, click here. This post originally ran on stefanmikarlsson.blogspot.com.
[More from Mashable: 10 Explosive iPhone Fireworks Photos [PICS]]
UPDATE: We've made three attempts to contact Apple officials, trying to find out what this "replacement unit" will be if you send in a first-generation iPod Nano. There has been no response. We called Apple support, asking if a new iPod Nano would be sent to replace the 5-year-old Nanos. Here's the response the company is giving to its customers: "Your guess is as good as mine." Stay tuned for a full story, whether Apple officials respond or not.
[More from Mashable: 10 Geeky Accessories Celebrating the Iconic Hand Cursor [PICS]]
UPDATE 2: Confirmed (finally): First-generation iPod Nanos will be sent as replacements. Read the story here.
Do you have an old first-generation iPod Nano lying around? If so, Apple wants to replace it for you, 5 years after you bought it. Such a deal.
But watch out: There's a slight risk of your old Nano overheating, and possibly even catching on fire because of a defective battery. Apple says if you own one of the Nanos with this problem, you should stop using it immediately. The good news is, newer iPods aren't affected by the battery defect.
Writes the company on its website:
"Apple has determined that, in very rare cases, the battery in the iPod nano (1st generation) may overheat and pose a safety risk. Affected iPod Nanos were sold between September 2005 and December 2006.
This issue has been traced to a single battery supplier that produced batteries with a manufacturing defect. While the possibility of an incident is rare, the likelihood increases as the battery ages."
Apple's providing a place to check your Nano's serial numbers and order a "replacement unit." So far, it's unclear exactly what Apple will send you if you have the correct serial number on your old Nano. We presume the company wouldn't dig up old iPod Nanos from the distant past, nor would it swap out the batteries in the one you have now.
So if our guess is correct, you'll be able to trade in that old beat-up and scratched-up iPod for a shiny new one. We've contacted the company to find out, but we can't imagine Apple sending anything but the Read our story here.
We'll update this post if and when we hear from Apple. In the meantime, start digging around in those old dresser drawers -- there might be an old iPod in there for you to cash in on a new one.
ROME ? Market pressure on Italy eased somewhat Thursday after the president vowed to accelerate reforms to make way for Premier Silvio Berlusconi's resignation as early as this weekend and a bond sale went better than expected.
President Giorgio Napolitano assured skittish investors that Berlusconi will step down after reforms are passed ? likely by Saturday ? and he named respected economist Mario Monti senator for life in a move that puts him in line to run the next government.
Italy is under intense pressure to prove it has the political strength to enact measures to increase confidence in its ability to repay its debts, which stand at a huge 120 percent of economic output. But economic growth is weak and the government has been incapable of pushing through reforms to revive it over the past decade.
Italy's leading business newspaper summed up the growing sentiment with an enormous bold-faced headline: "Hurry Up."
Investors are worried that if Italy's borrowing rates remain too high for too long, it will be blocked out of financial markets and need rescue loans to repay its bondholders. That would be devastating for both the euro and the global economy.
The yield on the benchmark 10-year bonds dropped below 7 percent on Thursday after a bond sale went better than expected. The yield had spiked to almost 7.5 percent on Wednesday, topping the threshold that eventually forced Greece, Ireland and Portugal to seek bailouts. By midday Thursday it had eased back down to 6.94 percent.
Italy easily sold euro5 billion ($6.8 billion) in 12-month bonds at borrowing rates which were not as bad as expected. Investors asked for an interest rate of 6.087 percent to lend Italy the 12-month money. That's up sharply from 3.57 percent in the last such auction last month, but well below analyst expectations of 7 percent. Demand for the bonds was also strong, almost twice the amount on sale.
Indications that Monti, a leading economist who heads Milan's Bocconi University, would head a new government brought some relief, but many details still need to be worked out.
The elegant, gray-haired Monti, 68, made his reputation as a strong-willed economist when as EU competition commissioner he blocked General Electric's takeover of Honeywell.
Berlusconi's designated successor Angelino Alfano indicated on Italian TV that the premier would step down between Saturday and Monday, and that he would accept Monti. But the allied Northern League, a key element of Berlusconi's government, is staunchly opposed to a government of technocrats.
The main opposition parties appear to be in line to accept Monti as the head of a broad-based government of technocrats, however some more hard-line elements of the left, including unions, remain opposed.
Antonio Di Pietro, a former prosecutor who heads a small left-wing party, said his party would not support Monti.
Financial chaos reverberated around the world, and investors pulled money out of Europe and stock markets fell.
Investors fear Italy might follow Greece, Ireland and Portugal into begging for a bailout from its partners in the euro. But Italy's euro1.9 trillion ($2.6 trillion) debt is far too great for Europe to cover.
Berlusconi announced Tuesday he would step down after Parliament passes a series of economic reforms to stave off financial ruin in Italy. But markets worried the tenacious premier will try to stay in power.
Parliamentary whips feverishly worked out a timetable to ensure that the Italian Senate would give final approval Friday to the package of measures, aimed at stimulating growth and reining in debt, according to state TV. It said the lower house would do the same on Saturday, meaning Berlusconi could be out before the weekend is over.
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Public release date: 15-Nov-2011
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