9. Which of the following non-covalent interactions could the sidechain of F266 participate in. Place an "X" next to all that apply. lonic (or salt bridge or charge-charge) Hydrogen bond Dipole-dipole Dipole-induced dipole Induced dipole-induced dipole Charge-dipole Charge-induced dipole П-stacking 10. The thermodynamic values for the folding of a protein are as follows: AG° = -38 kJ/mol = AH° = -164 kJ/mol AS -0.68 kJ/K.mol Which one of the following statements is most likely true? Circle your answer. A. Folding of this protein is primarily driven by the formation of favorable noncovalent interactions in the folded protein. B. Folding of this protein is primarily driven by the formation of hydrogen bonds between the protein and the bulk solvent (water). C. Folding of this protein is primarily driven by the loss of conformational entropy in the folded protein. D. Folding of this protein is primarily driven by the gain of conformational entropy in the folded protein. E. Folding of this protein is primarily driven by the loss of entropy in the bulk solvent (water). F. Folding of this protein is primarily driven by the gain of entropy in the bulk solvent (water).

9. Which of the following non-covalent interactions could the sidechain of F266 participate in. Place an "X" next to all that apply. lonic (or salt bridge or charge-charge) Hydrogen bond Dipole-dipole Dipole-induced dipole Induced dipole-induced dipole Charge-dipole Charge-induced dipole П-stacking 10. The thermodynamic values for the folding of a protein are as follows: AG° = -38 kJ/mol = AH° = -164 kJ/mol AS -0.68 kJ/K.mol Which one of the following statements is most likely true? Circle your answer. A. Folding of this protein is primarily driven by the formation of favorable noncovalent interactions in the folded protein. B. Folding of this protein is primarily driven by the formation of hydrogen bonds between the protein and the bulk solvent (water). C. Folding of this protein is primarily driven by the loss of conformational entropy in the folded protein. D. Folding of this protein is primarily driven by the gain of conformational entropy in the folded protein. E. Folding of this protein is primarily driven by the loss of entropy in the bulk solvent (water). F. Folding of this protein is primarily driven by the gain of entropy in the bulk solvent (water).

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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