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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 ?
The chicken breast fillets (Pectoralis major m.) from left sides were collected and stored in a cold room at 5[degrees]C and then submitted to analysis of color (L*, a*, and b*), pH, Warner-Bratzler (WB) shear force, water holding capacity (WHC), emulsification capacity (EC), protein denaturation (PD), fatty acid profile and Fourier-transform infrared spectroscopy in an attenuated reflectance mode (FTIR-ATR) at 24 h post-mortem.
The increase in lipid peroxidation supports the decrease in protein denaturation and the total protein volume.
(2015) reported the effect of freezing and thawing process on protein denaturation, color changes and oxidation of protein and lipid in meat.
Extreme temperatures cause severe cell damage due to irreversible protein denaturation (Hamdoun et al., 2003; Li et al., 2007; Farcy et al., 2009).
SEC aggregate analysis is commonly used to quantify the extent of protein denaturation that may have occurred during production or storage.
Measurements will include temperature/ species forming in collapsing bubbles, Identifying chemical reactions and possible tissue interaction, Such as protein denaturation and agglomeration; Tissue cavitation threshold and its control using nanoparticles, Allowing development of new cavitation-mimicking-tissue materials extrapolating to actual tissue properties that will be used for in-vitro testing of equipment with minimum collateral damages.
During sonication, the cells were incubated in ice and 1 mM PMSF was added to avoid protein denaturation. The ruptured membranes were collected by centrifugation at 17,000 rpm maintained at 4 [degrees]C for 1 h and resuspended in 3 ml of 1% Sarkosyl (HiMedia, India) in 10 mM Tris-Cl solution and incubated overnight at 4 [degrees]C.
Texture changes during frozen storage have also been directly linked to protein denaturation within fish [58].
Surface hydrophobicity can be a suitable parameter to estimate protein denaturation, and higher protein surface hydrophobicity represents more protein denaturation [17].
Nevertheless, as Lyubarev and Kurganov noted in [34], that experimental data are satisfactorily described by the two-state model, the real mechanism of protein denaturation can be more complex.
The decrease in protein solubility is used as an indicator of protein denaturation. Decreases in solubility might be caused by protein aggregation during frozen storage or the freeze-thaw process [40].