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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]
Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). [1] The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. [1]
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
Coagulation occurs as a result of protein denaturation, causing albumin to transform into a firm and opaque state. [6] This pattern of necrosis is typically seen in hypoxic (low-oxygen) environments, such as infarction. Coagulative necrosis occurs primarily in tissues such as the kidney, heart and adrenal glands. [6]
Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding.
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.
The discipline of anatomy can be subdivided into a number of branches, including gross or macroscopic anatomy and microscopic anatomy. [10] Gross anatomy is the study of structures large enough to be seen with the naked eye, and also includes superficial anatomy or surface anatomy, the study by sight of the external body features.
Ovalbumin is the most abundant protein in albumen. Classed as phosphoglycoprotein, during storage, it converts into s-ovalbumin (5% at the time of laying) and can reach up to 80% after six months of cold storage. Ovalbumin in solution is heat-resistant. Denaturation temperature is around 84 °C, but it can be easily denatured by physical stresses.