Explain in detail how protein folding is a thermodynamically favored process even though the change in entropy is highly unfavorable.
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- The process of protein folding is spontaneous in the thermodynamic sense. It gives rise to a highly ordered conformation that has a lower entropy than the unfolded protein. How can this be?Denatured protein is in a low energy state. What sort of explanation can you use to rationalize that statement? Hint: consider Gibbs free energy.List three effects of macromolecular crowding on the properties of enzymes and the reactions they catalyze.
- Discuss the behavior of enzymes as described by the Michaelis-Menten EquationConsider an enzyme catalyzed reaction taking place in an aqueous solution. If the earlier process of folding the enzyme results in a large decrease in the entropy of the system, how would this impact the rate of the catalyzed reaction.Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red.
- Which of the following statements are correct about the thermodynamics of protein folding (select all that appy)? A. The deltaG for protein folding is negative B. Burial of hydrophobic side provides a positive entropy change that drive protein folding C. The overall entropy change of protein folding is favorable D. Intercations between amino acids provide a large negative deltaH that helps favor the native state. E. The free energy change of protein folding is dependent on the temperatureBriefly describe the role of the heat shock protein Hsp70 in protein folding.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.
- Which has greater conformational entropy, a folded protein, or an unfolded one? Actually can you please explain about conformational entropy??Explain briefly why the ionizable properties of amino acids are so crucial in the structure and function of proteins.Which way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceeds