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term used to describe the loss of native, higher-order structure of proteinprotein,
any of the group of highly complex organic compounds found in all living cells and comprising the most abundant class of all biological molecules. Protein comprises approximately 50% of cellular dry weight.
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 molecules in solution. Most globular proteins exhibit complicated three-dimensional folding described as secondary, tertiary, and quarternary structures. These conformations of the protein molecule are rather fragile, and any factor that alters the precise geometry is said to cause denaturation. Extensive unfolding sometimes causes precipitation of the protein from solution. Denaturation is defined as a major change from the original native state without alteration of the molecule's primary structure, i.e., without cleavage of any of the primary chemical bonds that link one amino acid to another. Treatment of proteins with strong acids or bases, high concentrations of inorganic salts or organic solvents (e.g., alcohol or chloroform), heat, or irradiation all produce denaturation to a variable degree. Loss of three-dimmensional structure usually produces a loss of biological activity. Thus, the denatured enzymeenzyme,
biological catalyst. The term enzyme comes from zymosis, the Greek word for fermentation, a process accomplished by yeast cells and long known to the brewing industry, which occupied the attention of many 19th-century chemists.
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 is often without catalytic function. Renaturation is accomplished with varying success, and occasionally with a return of biological function, by exposing the denatured protein to a solution that approximates normal physiological conditions. Denaturation may be studied in the laboratory in any number of ways that monitor the physical properties of protein. Thus measurements of changing viscosity, density, light-scattering ability, and movement in an electrical field all record slight changes in molecular architecture. Denaturing is also used to describe the unrelated process of adding a poisonous substance to ethanolethanol
or ethyl alcohol,
CH3CH2OH, a colorless liquid with characteristic odor and taste; commonly called grain alcohol or simply alcohol. Properties

Ethanol is a monohydric primary alcohol. It melts at −117.
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 to make it unsuitable for human consumption.
References in periodicals archive ?
When 83[degrees]C or 82[degrees]C denaturation for 10 s were set as the [T.
The cDNA was amplified using an Eppendorf-gradient PCR thermal cycler using the following parameters: initial DNA denaturation at 95[degrees]C for 5 minutes, followed by 35 cycles of 95[degrees]C denaturation for 1 minute, annealing temperatures ranging from 51[degrees]C to 71[degrees]C for 1 minute, elongation at 72[degrees]C for 1 minute, and final elongation of 72[degrees]C for 7 minutes, followed by cooling at 4[degrees]C.
On denaturation, the digestibility of the soy protein may improve.
The presence of identical HDs in Group II and Group III as shown on Figure 1 leads to a conclusion that a single denaturation step in absence of primers is sufficient for detection of HDs.
The energy required for denaturation of protein is approximately equal to free energy (?
The thermal study of mixtures and produced films denaturation was performed on a Pyris 1 power modulation Differential Scanning Calorimeter (Perkin Elmer), equipped with an Intracooler.
The micronization process prevents the beans from losing their flavor as a result of heat denaturation.
The thermal cycling conditions consisted of an initial denaturation step at 95[degrees]C for 10 min and 40 cycles at 95[degrees]C for 15 sec and 60[degrees]C for 1 min.
Because of these constraints, it is difficult to integrate enzymatic catalysts into industrial processes where they are prone to denaturation as a result of harsher prevailing conditions.
In 1993 we came up with the revolutionary idea of refolding proteins by exposing them to a series of denaturation and renaturation steps, and the method resulted in a drastic improvement in the yield of correctly folded protein," said Hans Christian Thogersen, Borean's Chief Scientific Officer and Founder.
While it is believed that denaturation of adsorbed proteins at the implant surface directly leads to the adhesion and activation of platelets and subsequent thrombus formation, no data exists to directly correlate these two phenomena.