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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]
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. In situations of excess protein intake, deamination is used to break down amino acids for energy.
Family 1 includes Stearoyl-CoA desaturase-1 (SCD) (EC 1.14.19.1). [17] Family 2 is composed of: Bacterial fatty acid desaturases. Plant stearoyl-acyl-carrier-protein desaturase (EC 1.14.19.1), [18] an enzyme that catalyzes the introduction of a double bond at the delta-9 position of steraoyl-ACP to produce oleoyl-ACP. This enzyme is responsible ...
Parts-per-million cube of relative abundance by mass of elements in an average adult human body down to 1 ppm. About 99% of the mass of the human body is made up of six elements: oxygen, carbon, hydrogen, nitrogen, calcium, and phosphorus. Only about 0.85% is composed of another five elements: potassium, sulfur, sodium, chlorine, and magnesium ...
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.
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.
Post-translational modifications can occur before protein folding or after. Common biological methods of modifying peptide chains after translation include methylation, phosphorylation, and disulfide bond formation. Methylation often occurs to arginine or lysine and involves adding a methyl group to a nitrogen (replacing a hydrogen).
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 (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses