protein after denaturation can be renatured explain with example
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Explanation:
Some of the smaller proteins, however, are extremely stable, even against heat; for example, solutions of ribonuclease can be exposed for short periods of time to temperatures of 90 °C (194 °F) without undergoing significant denaturation. Denaturation does not involve identical changes in protein molecules. A common property of denatured proteins, however, is the loss of biological activity—e.g., the ability to act as enzymes or hormones.
Although denaturation had long been considered an all-or-none reaction, it is now thought that many intermediary states exist between native and denatured protein. In some instances, however, the breaking of a key bond could be followed by the complete breakdown of the conformation of the native protein.
Although many native proteins are resistant to the action of the enzyme trypsin, which breaks down proteins during digestion, they are hydrolyzed by the same enzyme after denaturation. The peptide bonds that can be split by trypsin are inaccessible in the native proteins but become accessible during denaturation. Similarly, denatured proteins give more intense colour reactions for tyrosine, histidine, and arginine than do the same proteins in the native state. The increased accessibility of reactive groups of denatured proteins is attributed to an unfolding of the peptide chains.
The motion of protein molecules at the air–water interface has been used to determine the molecular weight of proteins. The technique involves measuring the force exerted by the protein layer on a barrier.
When a protein solution is vigorously shaken in air, it forms a foam, because the soluble proteins migrate into the air–water interface and persist there, preventing or slowing the reconversion of the foam into a homogeneous solution. Some of the unstable, easily modified proteins are denatured when spread in the air–water interface. The formation of a permanent foam when egg white is vigorously stirred is an example of irreversible denaturation by spreading in a surface.