Molecular chaperones in cellular protein folding

Article Abstract:

Molecular chaperone proteins of the heat-shock protein 70 (Hsp70) and chaperonin families stabilize newly formed polypeptides by binding to them, and controled release of the polypeptides regulates protein folding, degradation, transport or oligomeric assembly. The Hsp70 proteins and ATPases function during both normal and stress conditions. The binding and release of proteins by the Hsp70 proteins is regulated by proteins such as Hsp40. The J-domain of Hsp40 proteins is involved in the interaction of Hsp70 and Hsp40 proteins.

Reports, Physiological aspects, Heat shock proteins, Protein folding

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Recycling the past

Article Abstract:

Nuclear-fuel reprocessing aims to reduce the volume of spent nuclear fuel that has to be disposed to safety by recycling it for use in new types of nuclear reactor. But the recycling involves separating components that could readily be used to build nuclear weapons.

United States, Nuclear Energy Products, All Other Basic Inorganic Chemical Manufacturing, CHEMICALS AND ALLIED PRODUCTS, Nuclear Fuel, Pollutants produced & recycled, Environmental aspects, Nuclear fuels, Waste management, Materials, Nuclear reactors

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