Desirable defects in liquid crystals
Making magnetic hot spots with pairs of silicon nanocylinders
Harnessing sunlight more effectively with nanoparticles
Physics of heavy ion induced damage in nanotwinned metals revealed
How to grow nanostructures in a controlled manner on a variety of metals
Developing portable, highly sensitive gold detection down to nanoparticles
A new constitutive model for the thermo-elasto-plasticity deformation of crystals
When mediated by superconductivity, light pushes matter million times more
Random light scattering enhances the resolution of wide-field optical microscope images
Graphene-based technique creates the smallest gaps in nanostructures
Researchers model new atomic structures of gold nanoparticle
Study explores the interaction of carbon nanotubes and the blood-brain barrier
Simpler nanoscale bioreplication of beetle decoys
Graphene brings 3-D holograms clearer and closer
Chemists' synthesis of silicon oxides opens 'new world in a grain of sand'
Gregory H. Robinson is the University of Georgia Foundation Distinguished Professor of Chemistry. The study, published April 20 in the journal ("Stabilization of elusive silicon oxides"), gives details on the first time chemists have been able to trap molecular species of silicon oxides.
Using a technique they developed in 2008, the UGA team succeeded in isolating silicon oxide fragments for the first time, at room temperature, by trapping them between stabilizing organic bases.
"In the 2008 discovery, we were able to stabilize the disilicon molecule, which previously could only be studied at extremely low temperatures on a solid argon matrix," said Gregory H. Robinson, UGA Foundation Distinguished Professor of Chemistry and the study's co-author. "We demonstrated that these organic bases could stabilize a variety of extremely reactive molecules at room temperature."
The columns, or groups, of elements of the periodic table generally share similar chemical properties. Group 14, for example, contains the element carbon, as well as silicon, the most carbon-like of all the elements. However, there are significant differences between the two. While the oxides of carbon, carbon dioxide and carbon monoxide are widely known, the molecular chemistry of corresponding silicon oxides is essentially unknown, due to the great reactivity of silicon-oxygen multiple bonds.
A light switch for superconductivity
Ultra-sensitive sensor detects individual electrons
Scientists use nanoscale building blocks and DNA 'glue' to shape 3D superlattices
Mechanical cloaks of invisibility - without complicated mathematics
Low-reflection, nanostructured wings make butterflies nearly invisible
Surface matters: Huge reduction of heat conduction observed in flat silicon channels
Nanoscientists model atomic structures of three bacterial nanomachines
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The finding confirms how the disease affects cells. When healthy cells encounter nanoscale objects in the body, they assume the objects are nutrients and absorb them. Like a Trojan horse, the toxin pore appears to the cells as something beneficial — in this case, a nutrient — and is taken in by the cell. But once inside the cell, the pore senses the change to a more acidic environment, which opens the pore’s gate and releases the anthrax toxin molecule into the cell. “This is a very important step toward understanding this mechanism, and it is essential for any anthrax countermeasure,” Zhou said. “It also informs our understanding of the mechanisms of other toxins that function like anthrax, which could lead to other targeted antibiotic drugs.” Tularemia type VI secretion system Another nanomachine was described by Dr. Marcus Horwitz, a UCLA professor of medicine and of microbiology, immunology and molecular genetics, who worked with Zhou’s team. In a study published in the journal ("Atomic Structure of T6SS Reveals Interlaced Array Essential to Function"), the scientists reported the first atomic resolution model of any type VI secretion system, or T6SS, a nanomachine found in roughly 25 percent of gram-negative bacteria. Gram-negative bacteria are responsible for diseases such as cholera, salmonellosis, Legionnaires’ disease and melioidosis, and severe infections including gastroenteritis, pneumonia and meningitis. For the new study, the scientists examined Francisella tularensis, a bacterium that causes tularemia and is of great concern as a potential bioterrorism agent. Built from component proteins, the T6SS nanomachine has an atomic structure that resembles a piston. When F. tularensis is taken up into a type of white blood cell called a macrophage it is surrounded by a bubble-like membrane, a structure known as a phagosome. The T6SS nanomachine then assembles inside the bacterium, where it plunges a tube through the bacterial wall and the membrane of the phagosome into the cytoplasm, the substance inside the macrophage. This enables the bacterium to escape the phagosome into the cytoplasm, where it can complete its lifecycle and multiply. Soon, the macrophage fills with bacteria and ruptures, freeing the bacteria to infect other cells. Thus, the T6SS is a novel target for antibiotics against this bacterium, and against others that use it to survive within host cells or to combat rival bacteria. “We are already identifying drug molecules that target the F. tularensis T6SS,” Horwitz said. “Knowing how this structure works guides us in selecting drug molecules that block its assembly or function. The overall goal is to find new antibiotics that directly target this top-tier bioterrorism agent and other gram-negative bacteria with a T6SS such as Vibrio cholerae, Pseudomonas aeruginosa, Burkholderia pseudomallei, and pathogenic Escherichia coli.” Horwitz and his team could potentially also develop wider-spectrum drugs that work on many different gram-negative pathogens that have in common a T6SS. Pseudomonas aeruginosa In humans and animals, a bacterium called Pseudomonas aeruginosa causes infectious diseases that lead to generalized inflammation and sepsis, a dangerous infection of the blood. A team led by Zhou and Miller discovered the atomic structures of R-type pyocins, contractile ejection systems of Pseudomonas aeruginosa. Their findings were published online by ("Atomic structures of a bactericidal contractile nanotube in its pre- and postcontraction states"). R-type pyocins are used by the bacterium to rapidly insert their nanotubes, like battering rams, into the cell membranes of competing bacteria to kill the competitors, giving Pseudomonas aeruginosa easier access to nutrients. These pyocins appear to create a channel in the outer envelope of the target bacteria, which essentially acts to weaken and kill it. This ability has made R-type pyocins the focus of research into possible antimicrobial and bioengineering applications, and scientists believe they could be engineered to give drugs a powerful antibacterial component.[embedded content]
“The R2 pyocin is an extraordinary molecular machine that uses energy from its own biological battery to function,” said Miller, who also is a professor of microbiology, immunology and molecular genetics. “It is ideal for engineering targeted antibiotics that kill the bad bacteria without disrupting a patient’s protective gut bacteria.” The scarcity of the technology and the expertise needed to use it make CNSI one of the world’s few facilities capable of imaging atomic structures like these nanomachines at atomic-level resolution, which is why researchers from around the world come to UCLA to use the Electron Imaging Center for Nanomachines, a fee-for-service laboratory open to any scientist in academia or industry.