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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]
Hyperchromicity can be used to track the condition of DNA as temperature changes. The transition/melting temperature (T m) is the temperature where the absorbance of UV light is 50% between the maximum and minimum, i.e. where 50% of the DNA is denatured. A ten fold increase of monovalent cation concentration increases the temperature by 16.6 °C.
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.
Nucleic acid thermodynamics is the study of how temperature affects the nucleic acid structure of double-stranded DNA (dsDNA). The melting temperature (T m) is defined as the temperature at which half of the DNA strands are in the random coil or single-stranded (ssDNA) state.
Coagulative necrosis is characterized by the formation of a gelatinous (gel-like) substance in dead tissues in which the architecture of the tissue is maintained, [7] and can be observed by light microscopy. Coagulation occurs as a result of protein denaturation, causing albumin to transform into a firm and opaque state. [6]
Denaturation may refer to: 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 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 ...
Denaturation Mapping is a form of optical mapping, first described in 1966. It is used to characterize DNA molecules without the need for amplification or sequencing . It is based on the differences between the melting temperatures of AT-rich and GC-rich regions. [ 1 ]