Denaturation of protein is defined as the alternation of the native structure of a biopolymer causing a loss of biological activity. The biological activity of a biopolymer is closely related to the native structure of the biopolymer. This can remain intact only if some crucial factors such as the temperature, the level of acidity of a solution in terms of hydrogen activity (pH), the solvent and the solute are kept within certain limits.
Denaturation, however, does not modify the primary structure of the biopolymer. Proteins can be denaturated with the help of chaotropic agents such as urea and guanidine hydrochloride, detergents, heat and reagents. It is possible, under appropriate conditions, to reverse the process of denaturation of various types of proteins. For instance, it is possible to reverse the process of denaturation in the case of a protein called lysozyme. Until 1961, it was considered to be impossible to denature nucleic acids.
Denaturation, however, does not modify the primary structure of the biopolymer. Proteins can be denaturated with the help of chaotropic agents such as urea and guanidine hydrochloride, detergents, heat and reagents. It is possible, under appropriate conditions, to reverse the process of denaturation of various types of proteins. For instance, it is possible to reverse the process of denaturation in the case of a protein called lysozyme. Until 1961, it was considered to be impossible to denature nucleic acids.
