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

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

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
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
Which has greater conformational entropy, a folded protein, or an unfolded one? Actually can you please explain about conformational entropy??
Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the above
Which of the following are involved in protein secondary structure? select one or more : a. van der waal forces b. Disulfide bridges c. Hydrogen bonds d. Peptide bonds
Consider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing? ____________________
At what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)
Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryoelectron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?
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
Proteins frequently form complexes in which 2, 3, 4, or even more individual proteins (“monomers”) interact specifically with each other via hydrogen bonds or electrostatic interactions. The entire assembly of proteins can act as one unit in solution, and this assembly is called the “quaternary structure” of the protein. Suppose you discover a new protein whose monomer molar mass is 25,000 g>mol. You measure an osmotic pressure of 0.0916 atm at 37 °C for 7.20 g of the protein in 10.00 mL of an aqueous solution. How many protein monomers form the quaternary protein structure in solution? Treat the protein as a nonelectrolyte.
Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.