January 16, 2012
Category: Computer science • technology transfer
YEDA Research and Development Company LTD., the commercial arm of the Weizmann Institute of Science, today announced it has entered into a license agreement with Adobe Systems Incorporated related to a bidirectional similarity measure to summarize visual data.
Here are some examples:
Before: 
After:
For more information, see our press release or Prof. Irani's website.
Read on »
Posted by Weizmann Science Writer at 1:05 AM • 0 Comments • 0 TrackBacks
January 11, 2012
Category: Archaeology • Scientific collaboration • Scientific equipment
Plaster from human dwellings or the signs of a long-abandoned animal enclosure? Tuesday's New York Times describes the collaboration between a chemist - structural biologist Prof. Steve Weiner, who is head of the Helen and Martin Kimmel Center for Archaeological Science at the Weizmann Institute - and American archaeologists. From China to the nearby site of biblical Gath, Weiner and his team have been applying the methods of advanced chemistry to solving riddles of the ancient world. (The answer, at least for the dig at Ashkelon, is fecal and decayed plant matter, meaning the apparent palace was really a stable.)
But even as that article appeared, hi-tech archaeology at the Institute was getting kicked up a fairly large notch. On Wednesday, the presidents of the Max Planck Society for the Advancement of Science and the Weizmann Institute, Profs. Peter Gruss and Daniel Zajfman, signed an agreement to open a new center for collaborative archaeology research. The research will be carried out at the Weizmann Institute of Science and the Max Planck Institute for Evolutionary Anthropology in Leipzig, Germany.
Among the technological wonders that will be used to reveal the microscopic finer points of relics from pottery to teeth will be a big-ticket piece of equipment that is being constructed especially for the purpose and is slated to be installed in a physics facility sometime this year. This accelerator mass spectrometer (AMS) can be used for radiocarbon dating with an accuracy of a few tens of years; and it can pick out one carbon atom in a quadrillion (ten to the 15th). According to Dr. Elisabetta Boaretto, the Kimmel Center's radiocarbon dating expert, it will be able to accurately date a single lentil or grain of wheat.
Other research will make use of Weiner's experience in investigating modern materials - specifically teeth. His studies of the microstructure of modern human teeth have revealed how they stand up to the daily pressures of chewing. Now, similar analyses will be used to examine the evolution of teeth in our nearest ancestors.
Posted by Weizmann Science Writer at 8:00 AM • 3 Comments • 0 TrackBacks
January 9, 2012
Category: Art and science • Brain and mind • Creativity • Neurobiology • Popular lectures
The actors on the stage work their magic, turning a few disparate phrases - "challenge, giving birth, infinity, chaos, visiting a new country" - into a brief but charming improvised sketch, to the delight of the audience. But the viewers, filling a large auditorium at the Weizmann Institute of Science, expect more than to be entertained. Since the improvised play is part of a lecture by Prof. Uri Alon, a Molecular Cell Biologist, they know scientific insights are bound to follow.
Indeed. Combining his two passions, science and theater, Alon has recently created a "theater lab" on the Weizmann campus, as part of the Institute's new Human Brain and Mind Program. The "lab" is a twice-weekly workshop that brings together Weizmann scientists and actors from the Kartoshkes Ensemble Playback Theater, in an attempt to subject to rigorous scientific analysis topics that are not always easy to define, let alone quantify - creativity, spontaneity, togetherness.
Read on »
Posted by Weizmann Science Writer at 3:42 AM • 0 Comments • 0 TrackBacks
December 27, 2011
Category: Autoimmune disease • Biochemistry • Biomedical • Drug design
Often, simply identifying the structure of a potential drug target protein and designing a molecule to block it are not enough. Just ask Prof. Irit Sagi, a chemist turned biology researcher, who recently developed a clever technique for directing the body to design its own protein-blocking molecules.
Sagi studies an enzyme called matrix metalloproteinase 9 (MMP-9). This protein, along with other members of the MMP family, cleaves straight through the support tissues in the body - collagen and the extracellular matrix that gives organs and tissues structure. This, of course is crucial for everything from wound healing to cell mobility but when dysregulated, MMP-9 in particular often finds its skills subverted to cancer metastasis and autoimmune syndromes. Sagi knows this protein inside out - she has investigated its active site, used innovative structural methods she developed in her lab to observe the dynamic conformations it goes through when activated, and identified weak points in the structure. Blocking the protein was not the main challenge. The problem lay in creating a selective molecule that would only block MMP-9 and not its many sister enzymes, all of which have a similar, metal-ion-based setup in their active sites. At least one small molecule blocker for this enzyme even made it to clinical trials, but the side effects were severe: Apparently it obstructed the activity of too many other MMP enzymes.
The idea for an alternative approach arose when Dr. Netta Sela-Passwell was an M.Sc. student on Sagi's lab. Instead of directly attacking the enzyme, the scientists looked for a way to trick the body's own regulatory system into stepping up activity. The plan was to design a synthetic molecule that would trigger an immune response against the metal-ion-based set up at the enzyme's active site.
left: natural enzyme blocker; right: novel antibody
In mice, the synthetic molecules Sagi and her lab team eventually created in collaboration with an organic chemistry group - pared-down versions of the enzyme's active site - performed as hoped: They significantly reduced symptoms of a Crohn's-like autoimmune disease. Interestingly enough, when the researchers checked the mice's blood, they found antibodies that were similar, but not identical to, inhibitors that the body normally produces to regulate the harmful activity of MMP-9. Testing these near-natural mouse antibodies on human versions of the enzyme revealed the same binding and blocking activity, and they only bound to one other member of the MMP family, rather than all of them.
Of course, the path from a method that works in mice to one that can be packaged as a drug for humans is long and treacherous. But Sagi and her team are excited by their finding - not just for its potential to treat a debilitating condition, but because it presents a whole new approach to dealing with human enzymes that are involved in promoting and abetting disease.
Posted by Weizmann Science Writer at 1:00 AM • 5 Comments • 0 TrackBacks
December 15, 2011
Category: Cloud computing • Computer science • Encryption
Is it possible to perform operations on encrypted data, while keeping it secure from all prying eyes (or circuits), even if that data is stored remotely, in the "cloud?" Will our end result still be encrypted, and when we decode it with our private decryption key, will our result be correct? To put it another way, could we allow sensitive data - say private medical information - to be monitored on-line and feel completely secure in the knowledge that no one can access it without our express permission? Can we use a cloud service to store our encrypted data and perform a search on that data without allowing the servers to "see" our search?
Welcome to the world of fully homomorphic encryption. The concept was first proposed in 1978 - long before the advent of remote computing services - by Rivest, Adelman and Dertouzos. (Rivest and Adelman, together with the Weizmann Institute's Prof. Adi Shamir, invented the RSA scheme used for almost all computer encryption today.) Since then, various researchers have come up with "partly homomorphic" methods, but none of them enabled full homomorphism. Only in 2009 was a fully homomorphic method demonstrated, by Craig Gentry at Stanford. That method, though proof of concept, was much too heavy and slow to be of any practical use.
Gentry published his method as his Ph.D. thesis. But it could be the doctoral work of another recent graduate - Dr. Zvika Brakerski from the Weizmann Institute (a student of Prof. Shafi Goldwasser) - that ultimately enables fully homomorphic encryption to become reality. Brakerski worked with Dr. Vinod Vaikuntanathan, a former student of Goldwasser's at MIT, who was at Microsoft Research at the time and is currently a professor at the University of Toronto.
In a nutshell: Gentry made some assumptions about the complexity of the math needed to achieve fully homomorphic encryption, and then used "a bit of a hack" (his words) to make it all work. Brakerski and Vaikuntanathan managed to change some of those assumptions (to "weaker" - more plausible and widely accepted - assumptions), simplifying the math and even eliminating the need for some of the hacks. The result, they say, is a method that is hundreds or even thousands of times faster than the original, but still fully homomorphic.
Brakerski, now doing postdoctoral research at Stanford, is continuing to research the math involved in fully homomorphic encryption. In the meantime, software engineers are already applying his insights to the future of data security.
Prof. Shafi Goldwasser and Dr. Zvika Brakerski
Also today at the Weizmann Institute:
White blood cells that reach into the blood vessel lining looking for "exit signs" and the closest supernova observation in the past 25 years yields new insights into how stars explode.
Posted by Weizmann Science Writer at 2:03 AM • 0 Comments • 0 TrackBacks
December 13, 2011
Category: ATLAS experiment • Announcements • CERN • Higgs boson
The Weizmann Institute's Prof. Eilam Gross is currently the ATLAS Higgs physics group convener. He originally wrote this piece in Hebrew for the Yediot Aharonot daily.
The Best There Is - For Now
"The God Particle," as the Higgs boson is often called, comes from the title of the book by Nobel laureate Leon Lederman that deals with the search for the elusive particle. This particle, according to the Standard Model of Particle Physics, is responsible for giving mass to all of the elementary particles in nature.
The mass of an electron determines the size of a hydrogen atom; ultimately the size of atoms ensures, amazingly enough, our existence. Maybe this is the reason the Higgs has been treated with almost mystical reverence in the mass media.
The Higgs boson is the only one of the elementary particles making up the Standard Model of Particle Physics that has not yet been discovered. Its importance can't be denied. Many scientists believe that the Standard Model will stand or fall on the discovery of Higgs boson particles or proof that they don't exist.
Three weeks ago, I attended a conference called "Higgs hunting" in Paris. Nearly everyone who is involved in the search for this particle was there. I was the guest of my friend Marumi Kado. At some point after a wonderful, wine-filled dinner, Marumi suggested a glass of grappa. "You must," he said. "It is Prime Uve, the best there is." A few hours later, in the wee hours of the morning, Marumi nudged me awake from a deep sleep and said: "Eilam, do you want to see a Higgs?" Of course, I jumped up immediately: "What? Where?" "The computer has stopped running; here are the results," he said. On his computer screen were images from CERN. We were all in shock. Something was out of the ordinary at a mass of 126 GeV (a unit of mass close to that of a proton). Definitely significant - 3.6 standard deviations. We couldn't believe our eyes - we looked at the screen for ages before we started to digest what we were seeing. For the past three weeks, the entire Higgs search team in the ATLAS experiment have checked and rechecked the results from every possible angle. We checked for errors... for bugs in the program.
fig.1
Read on »
Posted by Weizmann Science Writer at 10:13 AM • 3 Comments • 0 TrackBacks
December 12, 2011
Category: Chemistry • Education • Memory • Quasicrystals • Science event
If you followed this year's chemistry Nobel, you know about the quasicrystal design on the ties made for Prof. Dan Schechtman's 70th birthday. Even the prime minister was seen sporting one last week. But did you know there is also a quasicrystal scarf?
While Prof. Schechtman was getting his white tie and tails ready for the formal ceremony, this scarf was on display in fashionable Tel Aviv around the shoulders of Prof. Gitti Frey, a nanoscientist at the Technion.
Read on »
Posted by Weizmann Science Writer at 7:55 AM • 1 Comments • 0 TrackBacks
November 29, 2011
Category: Animal navigation • Ant society • Bat Brains • Biological networks • Neurobiology • Non-linear physics
This week's new Weizmann science stories are on ants and bats. Two different models for investigating human behavior? Yes, but not exactly in the ways you might imagine, and so much more than that.
Dr. Ofer Feinerman, the "ant scientist," is a new member of the Physics Faculty. In his graduate research under Prof. Elisha Moses in the Physics of Complex Systems Department, Feinerman created artificial circuits out of neurons. Now he has turned to investigating the complexities of ant societies. What, you might ask, do neurons and ant colonies have to do with physics? The answer is: They involve non-linear, collective phenomena, similar to those studied extensively by physicists. (Moses has investigated everything from falling leaves and advancing wave fronts* to schizophrenia to deep patterns in literature.) So in this physics lab, instead of lasers or ion traps, there are high-tech ant farms where the inhabitants run around with miniature barcodes glued to their backs.
Photo: Lab of Dr. Ofer Feinerman
Read on »
Posted by Weizmann Science Writer at 4:00 AM • 1 Comments • 0 TrackBacks
November 14, 2011
Category: Biophysics • Protein folding
Proteins are strung together from amino acids attached in long chains, one after the other. But for most proteins, this is just the beginning - next they must fold. "Folding" is the general term for the way that a protein strand twists, coils, winds, pleats and creases into an intricate three-dimensional structure. Only then can it go to work.
The sequence of amino acids is what determines the final shape of the protein: Molecules assembled on the same plan will end up in the exact same configuration. The funny thing is, they don't all go through the same set of steps to arrive at their final structure. Some of them, apparently, take shortcuts. It's as if you could skip a few steps in the origami instructions and still end up with a perfect paper crane in the end.
To observe and compare how individual protein strands fold, the Weizmann Institute's Prof. Gilad Haran and his team had to invent some new techniques, including fluorescent microscopy methods and data analysis that enabled them to collate thousands of individual events into a timeline of protein folding.
Experiments revealed multiple possible "paths" through a protein's folding landscape
The team identified six different intermediate configurations for the protein they studied. Sometimes the strands went through all of them; other times, they took an easier, shorter route to their final form.
Why would a molecule go through extra contortions to get to the same state? The findings contain a clue: The process became longer and more tortuous in the presence of some external factors such as heat or higher concentrations of certain chemicals in the protein's environment.
Like much good research, this study raises more questions than it answers: Is this a general rule that holds for different types of proteins? What advantages do the different routes to protein structure confer? How this might tie into such disorders as Alzheimer's disease, in which badly-folded proteins form plaques in brain tissue?
Posted by Weizmann Science Writer at 1:30 AM • 6 Comments • 0 TrackBacks
The Weizmann Institute of Science is a basic research institute in Rehovot, Israel. About 2,700 graduate students, scientists and staff work in 100 buildings on a 300-acre campus. There are five faculties: Biology, Biochemistry, Chemistry, Physics and Mathematics and Computer Science; as well as the Feinberg Graduate School and an educational arm – the Davidson Institute of Science Education
