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).

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.49P: 22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a...

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The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in the chain. Why is proline never present in a protein helix?
22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a substitution for leucine in the primary structure of a protein that would probably not change the character of the protein very much.
22-59 What is the effect of salt bridges on the tertiary structure of proteins?
Although the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.
Refer to the bar graph below, Explain why e.g. the n→π* interactions contribute more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why they contribute more than EACH bond.
The use of salt bridges or hydrophobic interactions (or pockets) to stabilize interactions between more distant amino acids within a single polypeptide, is a demonstration of protein TERTIARY structure. True False
Question 2. While internal cysteine amino acid sidechains in proteins undergo oxidation to produce disulfide crosslinks that stabilize the protein structure after folding, solvent-exposed cysteine sidechains can remain in their reduced thiol form and serve as reactive nucleophiles (recall for instance Acyl Carrier Proteins involved in fatty acid biosynthesis or various oxidoreductase enzymes). The reactive thiol groups in proteins can be detected using Ellman's test, wherein the protein is reacted with a disulfide Ellman's reagent to form a new mixed disulfide and a 2-nitro-5-thiobenzoate (TNB) byproduct. Upon addition of base, TNB is deprotonated to form a dianion, which absorbs light in the visible region and can be detected using UV-Vis spectroscopy. Ellman's Reagent CO₂H -NO₂ internal disulfide crosslink O₂N- HO₂C SH solvent- exposed thiol UV Absorbance at 412 nm O₂N- -S TNB²- alkaline pH O₂N- SH HO₂C 2-nitro-5-thiobenzoate (TNB) -NO2 mixed disulfide CO₂H a) Provide a detailed…
Describe the tertiary and quaternarystructure of a protein.
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. Why n→π* interactions contribute more to the overall stabilization of the protein than Sulfur-arene interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Anion-π interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Chalcogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than X-H-π interactions, even…
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein? * A. -CH3 В. -СH,ОН C. -CH,COO- D. -SH Е. -СH, CONH,
Examine the R groups of two amino acids illustrated below and specify the type of interaction that will occur between them in a protein tertiary or quaternary structure. -(CH,)-NH-C-NH, +NH₂ Arg Salt bridge C-CH₂ Asp O Hydrogen bond O Hydrophobic interaction O Disulfide bridge