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Scientists at the Scripps Research Institute and the University of Wisconsin have identified two small molecules with promising activity against neurotoxins produced by the Clostridium botulinum, a compound so deadly it has been labeled one of the six highest-risk bioterrorism agents by the Centers for Disease Control and Prevention.

Because of the high cost and limited applicability of currently available treatments, the newly identified compounds have the potential to fill the existing therapy gap and to provide protection against a bioterrorism attack using the toxin.

A Georgia Tech physics group has discovered how and why the electrical conductance of metal nanowires changes as their length varies. In a collaborative investigation performed by an experimental team and a theoretical physics team, the group discovered that measured fluctuations in the smallest nanowires’ conductance are caused by a pair of atoms, known as a dimer, shuttling back and forth between the bulk electrical leads. Determining the structural properties of nanowires is a big challenge facing the future construction of nanodevices and nanotechnology.

Two biologists at Penn State have discovered a master regulator that controls metabolic responses to a deficiency of essential amino acids in the diet. They also discovered that this regulatory substance, an enzyme named GCN2 eIF2alpha kinase, has an unexpectedly profound impact on fat metabolism.

Four million people die every year from respiratory diseases such as viral influenza. For elderly people in particular, an infection can be dangerous. What is more, the flu vaccine is not as effective with this risk group as it is with younger people. The reason for this is that with age the fire power of the immune system is reduced. Why this is the case is largely unknown. An international EU project led by the University of Bonn is now starting which aims at shedding light on this.

Researchers have constructed a protein out of amino acids not found in natural proteins, discovering that they can form a complex, stable structure that closely resembles a natural protein. Their findings could help scientists design drugs that look and act like real proteins but won't be degraded by enzymes or targeted by the immune system, as natural proteins are.

Researchers at the University of Illinois at Urbana-Champaign have developed a novel computational image-forming technique for optical microscopy that can produce crisp, three-dimensional images from blurry, out-of-focus data.

Many human proteins are not as good as they might be because the gene sequences that code for them have a double role which slows down the rate at which they evolve, according to new research published in PLoS Biology.

By tweaking these dual role regions, scientists could develop gene therapy techniques that produce proteins that are even better than those found in nature, and could one day be used to help people recover from genetic disorders.