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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
It is a medium-high to high heat cooking process. Temperatures between 160–190 °C (320–374 °F) are typical, but shallow frying may be performed at temperatures as low as 150 °C (302 °F) for a longer period of time. [1] The high heat promotes protein denaturation-browning and, in some cases, a Maillard reaction.
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
Dry heat sterilization of an object is one of the earliest forms of sterilization practiced. It uses hot air that is either free from water vapor or has very little of it, where this moisture plays a minimal or no role in the process of sterilization.
Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.
As the pH drops, proteins in the myofibers are denatured, leading to abnormal cell structure. The result is a pale tissue color, and a soft, almost mushy texture. The sarcomeres collapse excessively, and less water is held within the cell membrane and proteins. Subsequently, the myofibers will continue to lose water content as the meat is ...
Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses
Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. [5] The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.