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Protein denaturation occurs when the three-dimensional structures (in secondary, tertiary, or sometimes quaternary structures) of proteins is altered. Denaturation makes protein non-functional, or at least unable to perform its usual functions.
Protein - Denaturation, Structure, Function: When a solution of a protein is boiled, the protein frequently becomes insoluble—i.e., it is denatured—and remains insoluble even when the solution is cooled.
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 ...
Denaturation, in biology, process modifying the molecular structure of a protein. Denaturation involves the breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a protein molecule that are responsible for the highly ordered structure of the protein in its natural state.
The denaturation (unfolding) and renaturation (refolding) of a protein is depicted. The red boxes represent stabilizing interactions, such as disulfide linkages, hydrogen bonding, and/or ionic bonds. The primary structures of proteins are quite sturdy.
Protein denaturation refers to the change of the specific spatial conformation of protein in certain physical or chemical factors, resulting in the change of physical and chemical properties and loss of biological activity.
Denaturation is the process of breaking many of the weak bonds, such as hydrogen bonds, that give proteins their highly ordered structure when they are in their native, natural state. Weak and irregularly arranged, denatured proteins are mostly insoluble.
The denaturation (unfolding) and renaturation (refolding) of a protein is depicted. The red boxes represent stabilizing interactions, such as disulfide linkages, hydrogen bonding, and/or ionic bonds. The primary structures of proteins are quite sturdy.
Denaturation of the proteins is a condition when the unique three-dimensional structure of a protein is exposed to changes. Due to changes in temperature, pH or other chemical activities, the hydrogen bonds present in the proteins get disturbed.
The denaturation of proteins by a globule to coil transition is a classical subject of biophysics. 1 The thermal denaturation in which the protein goes from natural folded state to a random coil in aqueous solution occurs with raising temperature.