373. Which protein structure forms tight ß-sheets with alanine and glycine as major amino acids (a)globular (b) a-keratin (c) collagen (d) fibroin374. Folded proteins are (a) very stable (b) unstable (c) weakly stable375. Which side chain would be mainly found stabilizing protein quaternary structures?OHb. NH, Cd.NHỎ ĐOH

The precise three-dimensional arrangement of amino acids within a protein dictates its function and…

Answered: 373. Which protein structure forms…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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12. Consider a protein that can exist in two forms: folded (F) and unfolded (UF). Calculate the free energy of protein unfolding at 25 C (i) a state in which 70% of the protein is folded (ii) a state in which 90% of the protein is unfolded
5. Indicate whether the following amino acid residues would be more likely to be found on the surface or in the interior of a folded protein: Leu, Arg, Phe, Asn, and Glu. Give your reasoning for each case (diagrams not required).
1. Most globular proteins are denatured and lose their activity when briefly heated to 65°C. However, globular proteins that contain multiple disulfide bonds often must be heated longer and at higher temperatures to denature them. Furthermore, upon cooling of the denatured proteins, the activity of these proteins can often be restored. Explain these properties.
1. Hen Egg Lysozyme (HEL) is a commonly studied protein. One study reported that HEL unfolded at a "melting" temperature (TM) of 77.8 °C and calorimetric measurements determined the enthalpy for melting to be 500 kJ/mole. At the melting temperature, what are AG and AS°?
17. Protein folding results in a large decrease in entropy since a polypeptide is now constrained and more ordered. However, what counterbalances the loss of entropy associated with protein folding?
1. Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Suggestseveral features of proteins that drastically limit the actual number. 2. What are the greatest structural features that differentiate sphingolipids from phosphoglycerides? 3. High levels of glucose-6-phosphate inhibit glycolysis. If the concentration of glucose-6-phosphate decreases,activity is restored. Why?
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
1. Is there more than one way to fold a protein, given the conflicting demands of the different "R" groups and the protein existing in a watery environment? 2. Explain what an R group is. 3. Compare the backbone of a polypeptide with that of a nucleic acid. 4. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 5. Explain the difference between secondary and tertiary protein structures.
Misty Copeland is taking a snack break from her 8-hour rehearsal day and she wants to aid her muscles with recovery by eating a protein-rich snack. Part 1: What is the name of the monomer used to synthesize the protein and what is the name of the covalent bond that holds these monomers together? Part 2: The cells lining the inside of Misty Copeland's stomach need to produce and secrete enzymes like pepsin that will help breakdown the protein-rich snack she just ate. Using your knowledge of the endomembrane system (1) describe the pathway taken by the newly synthesized enzymes that will be secreted by her stomach cells? Include the terms cis-facing and trans-facing in your answer. (2) Include the type of cellular transport required for the enzyme to leave the cell. Part 3: The pH of Misty's stomach is low. For enzymes not used to this environment, which levels of protein structure will be affected? Briefly explain why the level(s) of structure you selected are being impacted. Part 4: If…
4. What type of tertiary structure interactions are most likely between the following amino acids? (Use a reference chart as necessary.) (b) methionine and methionine (a) glycine and valine (d) serine and lysine (c) cysteine and cysteine

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