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Explain why cooling denatured protein isn’t likely to reverse the effects of denaturization.

Explain why cooling denatured protein isn’t likely to reverse the effects of denaturization.

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Why cooling denatured protein is not likely to reverse the effects of denaturization

Denaturation

Denaturation of Protein which it's original shape gets destructed because of the breakage of chemical bonds which is already weak, and the separation of the interactions. Due to this effect Proteins become biologically inactive. It's inability to function is due to the disappearance of three dimensional structure, secondary, tertiary and quaternary structures. This leads to the changes even in the physical, chemical and biological properties of proteins. In simple, the conversion of well defined folded structure to unfolded state is called Protein Denaturation

Mainly reverse denaturation can be easily achievable, the reason is because of the facts that the amino acids which is held by the covalent bonds are in the exact sequel and the polypeptide primary structure. But this irreversibility is not possible in Cold denaturation of proteins.

Cold denaturation of proteins

The process in which the molecules are very stable at minimum temperatures and thermal fluctuations.

Cold denaturation causes limited unfolding of polypeptide chain. This leads to the alteration in the association of the water and hydrophobic groups. Falling off temperature results in the boosting of hydration. This is due to the decrease in the poor association of non polar residues with water. In other words, free energy cost for hydrophobic effect. Lower Temperature will result in diminishing hydrophobic effect and the depletion of tertiary structure.

Hydrogen bonds present in the interfacial water are more affirmative than the hydrogen bonds in the bulk water for cold denatured systems. Approximately this leads to the consideration of the unfolding process.

In Simple, Reduction in the flexibility will restrict the molecules from chemical reactions and binding nature with other molecules. When the temperature decreases the enzyme activity decreases, so it is not likely to reverse the effects of denaturisation.

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