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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]
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
In the earliest forms of denaturation mapping, DNA was denatured by heating in presence of formaldehyde [1] or glyoxal [3] and visualized using electron microscopy. Dyes that selectively bind to double stranded DNA like ethidium bromide could be used to monitor the extent of denaturation.
The most famous example is the hyperchromicity of DNA that occurs when the DNA duplex is denatured. [1] The UV absorption is increased when the two single DNA strands are being separated, either by heat or by addition of denaturant or by increasing the pH level. The opposite, a decrease of absorbance is called hypochromicity.
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).
3' untranslated region (3'-UTR). Also three-prime untranslated region, 3' non-translated region (3'-NTR), and trailer sequence.. 3'-end. Also three-prime end.. One of two ends of a single linear strand of DNA or RNA, specifically the end at which the chain of nucleotides terminates at the third carbon atom in the furanose ring of deoxyribose or ribose (i.e. the terminus at which the 3' carbon ...
A degmacyte or bite cell is an abnormally shaped mature red blood cell with one or more semicircular portions removed from the cell margin, known as "bites". [1] [2] These "bites" result from the mechanical removal of denatured hemoglobin during splenic filtration as red cells attempt to migrate through endothelial slits from splenic cords into the splenic sinuses. [3]
Even in the protein's denatured state, it can be folded into the correct structure. Globular proteins seem to have two mechanisms for protein folding, either the diffusion-collision model or nucleation condensation model, although recent findings have shown globular proteins, such as PTP-BL PDZ2, that fold with characteristic features of both ...