During the folding of a protein in a buffered aqueous solution, what happens to the entropy of the protein and the entropy of the water? The entropy of the protein decreases while the entropy of the water increases. Both the entropy of the protein and the entropy of the water increase. Both the entropy of the protein and the entropy of the water decrease. The entropy of the protein decreases while the entropy of the water remains constant.

During the folding of a protein in a buffered aqueous solution, what happens to the entropy of the protein and the entropy of the water? The entropy of the protein decreases while the entropy of the water increases. Both the entropy of the protein and the entropy of the water increase. Both the entropy of the protein and the entropy of the water decrease. The entropy of the protein decreases while the entropy of the water remains constant.

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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When a small, globular protein unfolds, which of the following are true? Choice 1 of 6:the temperature must increase Choice 2 of 6:the entropy of the peptide backbone increases Choice 3 of 6:the entropy of the solvent waters increases Choice 4 of 6:H bonds between peptide backbone atoms must break Choice 5 of 6:new attractive interactions form between water and side chains Choice 6 of 6:a detergent molecule must be added
When a small, globular protein unfolds, which of the following are true? (SELECT ALL THAT APPLY) Choice 1 of 6: the temperature must increase Choice 2 of 6: the entropy of the peptide backbone increases Choice 3 of 6: the entropy of the solvent waters increases Choice 4 of 6: H bonds between peptide backbone atoms must break Choice 5 of 6: new attractive interactions form between water and side chains Choice 6 of 6: a detergent molecule must be added
Choose all that apply: When a small, globular protein unfolds, which of the following are true? Choice 1 of 6:the temperature must increase Choice 2 of 6:the entropy of the peptide backbone increases Choice 3 of 6:the entropy of the solvent waters increases Choice 4 of 6:H bonds between peptide backbone atoms must break Choice 5 of 6:new attractive interactions form between water and side chains Choice 6 of 6:a detergent molecule must be added
What is the primary driver of protein folding on a macro level? a. Hydrogen bonding b. Van der Waals forces c. Covalent bonding d. Entropic force
Which of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.
Which has greater conformational entropy, a folded protein, or an unfolded one? Actually can you please explain about conformational entropy??
Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A. Covalent bonds B. Hydrogen bonds C. Van der Waals attraction D. Hydrophobic interactions
Which of the following is TRUE, if the protein pH is electrically neutral? Refer to the graph below. a. The denaturation of protein is lower than 100% b. The denaturation of protein is greater than 100% c. The protein is in native form d. The protein is completely denatured
Affinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the above
What level of protein structure is least likely to be affected if a protein's environment experiences a shift in pH below its optimal range? A. Quaternary B. Secondary C. Primary D. Tertiary
Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bonds
When a protein is folded in aqueous solution, some residues are driven inside to form a “hydrophobic core” which is far away from the water molecule. Which pair of the following residues are likely to be in the “hydrophobic core”? a. Gln and His b. Thr and Val c. Asp and Arg d. Ser and Tyr e. Ile and Leu

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		The entropy of the protein decreases while the entropy of the water increases.
		Both the entropy of the protein and the entropy of the water increase.
		Both the entropy of the protein and the entropy of the water decrease.
		The entropy of the protein decreases while the entropy of the water remains constant.