Two common methods of denaturing proteins in the lab are to increase the temperature and/or add chemical denaturants like the detergent SDS (shown below). Describe how each of these processes (heating and addition of SDS) disrupts the forces and interactions that stabilize the native state, leading to unfolding. The answer should include a discussion of the Gibbs free energy of folding, enthalpy, and entropy.
Two common methods of denaturing proteins in the lab are to increase the temperature and/or add
chemical denaturants like the detergent SDS (shown below). Describe how each of these processes
(heating and addition of SDS) disrupts the forces and interactions that stabilize the native state, leading
to unfolding. The answer should include a discussion of the Gibbs free energy of folding, enthalpy, and
entropy.
Proteins are biomolecules with diverse biological roles. The function of a protein depends on its three-dimensional structure, also called its native state. The loss of this three-dimensional structure is called the denaturation of protein. When denatured, the proteins fail to fulfil their biological role and are considered biologically inactive. Using heat and detergents such as SDS can effectively denature the protein.
The Gibbs free energy of folding is a measure of the stability of a protein's native state, which is dependent on both enthalpy and entropy.
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