A researcher at the Johns Hopkins Institute of Genetic Medicine has led the effort to compile to date the largest free resource of experimental information about human proteins. Reporting in the February issue of Nature Biotechnology, the research team describes how all researchers around the world can access this data and speed their own research.
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A detailed map that pinpoints the location of every atom in a 450-million-yeard-old resurrected protein reveals the precise evolutionary steps needed to create the molecule’s modern version, according to researchers from the University of North Carolina at Chapel Hill and the University of Oregon.
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Applying physical stress to cells, researchers at the University of Pennsylvania have demonstrated that everyday forces can alter the structure of proteins tucked within cells, unfold them and expose new targets in the fight against disease.
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In a paper published online this month in the journal Nature Chemical Biology, researchers report that they have developed a way to determine the function of some of the hundreds of thousands of proteins for which amino acid sequence data are available, but whose structure and function remain unknown.
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Our bodies could not maintain their existence without thousands of proteins performing myriad vital tasks within cells. Since malfunctioning proteins can cause disease, the study of protein structure and function can lead to the development of drugs and treatments for numerous disorders.
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Any photographer can vouch for the difficulty of capturing a clear picture of a moving target. When it comes to molecules, however, sometimes the motion is exactly what scientists want to see - for example, to understand the pathological protein mis-folding and assembly that seem to underlie a host of human disorders, including diabetes and Alzheimer's disease.
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How do blood clots maintain that precise balance of stiffness for wound healing and flexibility to go with the flow? Researchers at the University of Pennsylvania School of Medicine and the School of Arts and Sciences have shown that a well-known protein structure acts as a molecular spring, explaining one way that clots may stretch and bend under such physical stresses as blood flow.
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