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How are proteins denatured in an organic solvent?
Proteins can be denatured in organic solvents through disruption of the protein's structure due to the interactions between the solvent molecules and the protein. Organic solvents can disrupt the hydrogen bonds and hydrophobic interactions that stabilize the protein structure, leading to unfolding or denaturation of the protein. This can result in loss of the protein's biological activity.
Why does a denature protein no longer function normally?
the function of each protein is a consequence of its specific shape, which is lost when a protein becomes denatured.The shape of a protein determines its specific function within a cell. Denaturing a protein will alter its shape, thus it will no longer function.
What cellular organelle is responsible for recycling intracellular proteins?
The proteasome is responsible for degrading and recycling intracellular proteins that are damaged or no longer needed. This process helps to maintain cellular homeostasis by preventing the accumulation of misfolded or dysfunctional proteins.
What do pH and temperature alter the activity of an enzyme?
Enzymes are proteins, and proteins are designed to exist at specific temperatures and pH levels. When the temperature or the pH of their environment changes, the interactions that hold the amino acids of the enzyme in its particular conformation cease to function. The protein simply "falls apart" into an unstructured assembly of amino acids (a polypeptide still, but no longer a true protein) and cannot fulfill its function; this is called denaturation. For most enzymes, this occurs with an increase in temperature or a decrease in pH from their standard physiological environment.
Denaturation of proteins results in what?
Distortion of structure which could limit/remove its function(s).
