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There seems a real prospect that one of the infectious scourges of the past half century will not persist much beyond the present century, but polio will be only the second infection of human beings to be eradicated. Many more remain.
The case for modernizing the practice of medicine in the developing countries of the world is strong and also irresistible, but the mechanisms for doing that need to be improved.
The crystal structure of the trp RNA-binding attenuation protein of Bacillus subtilis solved at 1.8 Å resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit β-sheets to form a β-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent β-sheets in the β-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.
Here are some undiluted solutions to your immunology needs —an anti-fluoroscein single-chain antibody, monoclonal antibodies to Stat proteins 1–6 and a variety of microplate technologies.
