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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]
A 1991 assay for the Journal of Food Science detected substantial avidin activity in cooked egg white: "mean residual avidin activity in fried, poached and boiled (2 min) egg white was 33, 71 and 40% of the activity in raw egg white." The assay surmised that cooking times were not sufficient to adequately heat all cold spot areas within the egg ...
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.
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.
Also meganucleus. The larger of the two types of nuclei which occur in pairs in the cells of some ciliated protozoa. Macronuclei are highly polyploid and responsible for directing vegetative reproduction, in contrast to the diploid micronuclei, which have important functions during conjugation. macrophage Any of a class of relatively long-lived phagocytic cells of the mammalian immune system ...
Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases.. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney.
Folded, 3-D structure of ribonuclease A. Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology.It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence. [1]
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.