
How does denaturation affect the function of proteins?
Answer
554.7k+ views
Hint: Denaturation is the process by which a protein or nucleic acid loses its structure present in its native state (either quaternary, tertiary, or secondary) due to the use of some external stress or compound.
Complete answer:
Proteins are polymers made up of amino acids. They are produced in the cells by ribosomes. Denaturation of the proteins can be done by using many chemical compounds such as strong acid or alkali, inorganic salts, organic solvents, or by using a physical source such as radiation or heat. Denaturation of the proteins in living cells can even cause the death of the cells. Proteins that are denatured show a wide variety of characteristics such as a change in conformation.
The hydrogen bonds present in the proteins are weak, thus are easily broken by the effect of the above-mentioned factors. As denatured proteins lose their 3-dimensional structure, their functions are also hindered. Proteins must be folded in the right way to perform their functions accurately. The folding of proteins is balanced by a considerable amount of weak intramolecular interactions present within the protein molecule and the interaction between protein and the solvent. Thus, protein folding depends upon many factors such as pressure, salinity, temperature, and solvent. If the proteins are exposed to extreme conditions such as heat or radiations, or the presence of strong chemical compounds, the interaction is disrupted which leads to protein denaturation. Eventually, the protein can no longer perform its function. Many biological substrates such as enzymes, lose their activity, and can no longer make the substrate bind to the active site as their structure is changed.
Note: Mostly, denaturation is a reversible process as protein can regain their original structure once the reason for denaturation is removed. This process is known as renaturation.
Complete answer:
Proteins are polymers made up of amino acids. They are produced in the cells by ribosomes. Denaturation of the proteins can be done by using many chemical compounds such as strong acid or alkali, inorganic salts, organic solvents, or by using a physical source such as radiation or heat. Denaturation of the proteins in living cells can even cause the death of the cells. Proteins that are denatured show a wide variety of characteristics such as a change in conformation.
The hydrogen bonds present in the proteins are weak, thus are easily broken by the effect of the above-mentioned factors. As denatured proteins lose their 3-dimensional structure, their functions are also hindered. Proteins must be folded in the right way to perform their functions accurately. The folding of proteins is balanced by a considerable amount of weak intramolecular interactions present within the protein molecule and the interaction between protein and the solvent. Thus, protein folding depends upon many factors such as pressure, salinity, temperature, and solvent. If the proteins are exposed to extreme conditions such as heat or radiations, or the presence of strong chemical compounds, the interaction is disrupted which leads to protein denaturation. Eventually, the protein can no longer perform its function. Many biological substrates such as enzymes, lose their activity, and can no longer make the substrate bind to the active site as their structure is changed.
Note: Mostly, denaturation is a reversible process as protein can regain their original structure once the reason for denaturation is removed. This process is known as renaturation.
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