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Denaturation (food), the deliberate addition of an unpleasantly flavored or poisonous substances to food in order to prevent the consumption of the food for various reasons. Adulterant , a substance added to food for deceptive or malicious reasons, for example to cheaply replace legitimate ingredients.
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 is the process by which foods or liquids are made unpleasant or dangerous to consume; it is done by adding a substance known as a denaturant. Aversive agents —primarily bitterants and pungent agents —are often used to produce an unpleasant flavor.
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.
Similarly, RNA and single-stranded DNA can be run and visualised by PAGE gels containing denaturing agents such as urea. PAGE gels are widely used in techniques such as DNA foot printing, EMSA and other DNA-protein interaction techniques. The measurement and analysis are mostly done with a specialized gel analysis software.
The northern blot, or RNA blot, [1] is a technique used in molecular biology research to study gene expression by detection of RNA (or isolated mRNA) in a sample. [ 2 ] [ 3 ] With northern blotting it is possible to observe cellular control over structure and function by determining the particular gene expression rates during differentiation ...
A chaotropic agent is a molecule in water solution that can disrupt the hydrogen bonding network between water molecules (i.e. exerts chaotropic activity). This has an effect on the stability of the native state of other molecules in the solution, mainly macromolecules ( proteins , nucleic acids ) by weakening the hydrophobic effect .
The albumen from egg white was used as a binding agent in early photography during an 1855-90 period; such prints were called albumen prints. In the 1750s, egg whites were believed to prevent swelling, and were used for that purpose. To help soothe areas of skin that were afflicted, egg white mixed with Armenian bole could help restore the fibers.