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 deliberate addition of a noxious substance to alcohol to make it unfit to drink
The process of partial or total alteration of the native structure of a macromolecule resulting from the loss of tertiary or tertiary and secondary structure that is a consequence of the disruption of stabilizing weak bonds Denaturation can occur when proteins and nucleic acids are subjected to elevated temperature or to extremes of pH, or to non- physiological concentrations of salt, organic solvents, urea or other chemical agents [IUPAC Biotech]
the breaking down of the three-dimensional structure of a protein resulting in the loss of its function (23 1)
Destruction of the natural three-dimensional structure of large biological molecules (proteins or DNA), e g through heat In the case of DNA in particular, denaturation means the dissolution of the double strand into single strands
A process pertaining to a change in structure of a protein form regular to irregular arrangement of the polypeptide chains
{i} alteration or removal of natural properties; process by which alcohol is rendered unfit to drink
The change of folding structure of a protein (and thus of physical properties) caused by heating etc
1 The separation of the two strands of a double-stranded nucleic acid caused by treatments that overcome hydrogen bonding, e g heat 2 A usually irreversible change in the conformation of a protein caused by treatments that overcome hydrogen bonding, hydrophobic interactions, or other chemical forces that maintain the structure of proteins, e g heat
Irreversible destruction of a macromolecule, as for example the destruction of a protein by heat
Biochemical process modifying a protein's natural configuration. It involves breaking many weak (hydrogen and hydrophobic) bonds (see bonding) that maintain the protein's highly ordered structure. This usually results in loss of biological activity (e.g., loss of an enzyme's ability to catalyze reactions). Denaturation can be brought about by heating; treatment with alkalis, acids, urea, or detergents; or even vigorous shaking of the protein solution. It can be reversed in some cases (e.g., serum albumin, hemoglobin), if conditions favourable to the protein are restored, but not in others. The term is also used to describe the process of rendering ethanol unfit to drink
1 The separation of the two strands of a double-stranded nucleic acid caused by treatments that overcome hydrogen bonding, e g , heat 2 A usually irreversible change in the conformation of a protein caused by treatments that overcome hydrogen bonding, hydrophobic interactions, or other chemical forces that maintain the structure of proteins, e g , heat
the breaking down of the three-dimensional structure of a protein resulting in the loss of its function
1-The changing of a protein molecule, usually by the unfolding of the chains, to a less soluble state 2-To alter the original state of a food substance by physical or chemical means
the process of splitting the complementary double strands of DNA to form single strands
Process where double-stranded DNA unwinds and dissociates into two single strands The reverse of DNA-DNA hybridization
The lost of structural order and loss of function of a protein due to extreme pH, temperature or solvent conditions