4. 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. Your answer should include a discussion of the Gibbs free energy of folding, enthalpy, and entropy. Sodium dodecyl sulfate (SDS) O-Na+ MW 288

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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4. 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. Your answer should include a discussion of the Gibbs free energy of folding, enthalpy, and
entropy.
Sodium dodecyl sulfate (SDS)
O-Na+
MW 288
Transcribed Image Text:4. 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. Your answer should include a discussion of the Gibbs free energy of folding, enthalpy, and entropy. Sodium dodecyl sulfate (SDS) O-Na+ MW 288
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