Search results
Results from the WOW.Com Content Network
Definition of denaturation of protein. 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.
What is Denaturation of Proteins? Denaturation implies the destruction of the tertiary structure of a protein molecule and the formation of random polypeptide chains. Denaturation of proteins is one of the phenomenons that results in the disturbance of stability and structure of the protein.
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, 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.
Proteins unfold and become almost linear polypeptide chains upon denaturation. Denatured proteins can not perform their functions. Denaturation can be caused by heat, acids or bases, organic compounds and solvents, heavy metal ions, and agitation, as explained below.
A denatured protein cannot do its job. (Sometimes denaturation is equated with the precipitation or coagulation of a protein; our definition is a bit broader.) A wide variety of reagents and conditions, such as heat, organic compounds, pH changes, and heavy metal ions can cause protein denaturation.
denaturation: the change of folding structure of a protein (and thus of physical properties) caused by heating, changes in pH, or exposure to certain chemicals.
The study of protein unfolding/denaturation provides a considerable mass of information on stability, conformational dynamics, folding/unfolding intermediates, post-denaturation/renaturation events, and irreversible covalent modifications.
Proteins are denatured by treatment with alkaline or acid, oxidizing or reducing agents, and certain organic solvents. Interesting among denaturing agents are those that affect the secondary and tertiary structure without affecting the primary structure. The agents most frequently used for this purpose are urea and guanidinium chloride.
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 radiatio...