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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]
In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, pH, adding chemical denaturants, or applying force as with an atomic force microscope tip.
The effects of temperature on enzyme activity. Top - increasing temperature increases the rate of reaction (Q 10 coefficient). Middle - the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom - consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.
The external factors involved in protein denaturation or disruption of the native state include temperature, external fields (electric, magnetic), [36] molecular crowding, [37] and even the limitation of space (i.e. confinement), which can have a big influence on the folding of proteins. [38]
Temperature gradient gel electrophoresis (TGGE) and denaturing gradient gel electrophoresis (DGGE) are forms of electrophoresis which use either a temperature or chemical gradient to denature the sample as it moves across an acrylamide gel. TGGE and DGGE can be applied to nucleic acids such as DNA and RNA, and (less commonly) proteins.
Instead of a mechanical stopping system the reaction is stopped by quenching, the products being delivered to a recipient that stops the reaction immediately, either by instantaneous freezing or by denaturing the enzyme with a chemical denaturant or exposing the sample to a denaturing light source. As in the continuous-flow method, the time ...
Thermolabile enzymes are also studied for their applications in DNA replication techniques, such as PCR, where thermostable enzymes are necessary for proper DNA replication. Enzyme function at higher temperatures may be enhanced with trehalose , which opens up the possibility of using normally thermolabile enzymes in DNA replication.
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.