Research aids drug design; sheds light on plague and other diseases
A new technique for engineering protein crystals is helping scientists figure out the three-dimensional structures of some important biological molecules, including a key plague protein whose structure has eluded researchers until now. The technique, developed with support from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH), promises to help pharmaceutical companies develop more effective drugs to treat various diseases by tailor-making molecules to "fit" a proteins shape.
Featured in the cover article of the April 2004 issue of Structure, University of Virginia School of Medicine researcher Zygmunt Derewenda, Ph.D., describes how his group was able to coax certain proteins to crystallize by carefully altering their surfaces using "targeted mutagenesis." In effect, the technique substitutes a small amino acid for certain large ones. This effectively shrinks bulky groups of atoms on protein surfaces that might otherwise prevent the proteins from crystallizing.
Dan Hogan | EurekAlert!
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A study led by scientists of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg presents evidence of the coexistence of superconductivity and “charge-density-waves” in compounds of the poorly-studied family of bismuthates. This observation opens up new perspectives for a deeper understanding of the phenomenon of high-temperature superconductivity, a topic which is at the core of condensed matter research since more than 30 years. The paper by Nicoletti et al has been published in the PNAS.
Since the beginning of the 20th century, superconductivity had been observed in some metals at temperatures only a few degrees above the absolute zero (minus...
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