Enormous benefit for humans and without harming the environment can be extracted from domestic waste, old car wheel casings, industrial wastes and even silt, that remain after cleaning sewage outflows. It transpires that all this can successfully be turned into light and heat when incinerated, under methodology, developed by scientists from Chernogolovka in the Moscow Region, staff from the Institute of Problems of Chemical Physics RAS. The scientists were aided by the International Science and Technology Centre and the Russian Fund for Fundamental Research. The research is headed by RAS Corresponding Member Georgi Manelis.
This technology has a rather complicated name – filtration combustion with superadiabatic warm-up. The essence of the development lies in the fact that all of the so-called pseudo-fuel is first transformed to gas in an airflow; then this gas is combusted. As a result we get the same light and heat for which to date it has been necessary to literally let natural gas, coal and oil go up in smoke, fuel reserves which are far from endless in supply.
Externally the main part of the installation is a vertical shaft furnace, filled with these waste products that have to be processed. From below the pipe is blasted with air. This is where the ash is poured in – the mineral residue that does not burn at all. From above, as necessary, new portions of what in a domestic sense you would not call fuel are added into the pipe; these include poor coal, for example, in which there is so little carbon that you cannot make then burn easily.
Andrew Vakhliaev | alfa
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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