18.2 66. Taking into account all the possible conformations of the individual amino acid residues comprising a particularprotein, as the number of these conformations increases, conformational entropyA. DecreasesB. IncreasesC. Is unchangedD. Is undetermined67. Which of the following statements is FALSE regarding protein folding?A. The folding process for some proteins is facilitate by molecular chaperones.B. The presence of low stability regions in a protein allows it to change shapes.C. Thermodynamic factors like free energy and entropy affect protein folding.D. Thermodynamic stability is evenly distributed over the structure of a protein.68. Which of the following are generically associated to protein misfolding?A. Human genetic disordersB. Inborn errors of metabolismC. Neurodegenerative diseasesD. Spongiform encephalopathies

The amino acid sequence of a protein contains information that dictates its folding and ultimate…

Answered: Taking into account all the possible…

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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3. A. Briefly discuss the four levels of structure in proteins. Knowing that the 3-dimensional shape of a protein is important to its function, discuss on a qualitative basis whether the changes below will likely alter the function of a protein, justifying your answer with why or why not. B. What would happen to a protein's functionality if a serine residue were replaced with threonine? C. What would happen if serine were replaced with leucine? D. What would happen if serine were replaced with cysteine? E. What would happen if aspartic acid were replaced with tryptophan in the part of the protein (an enzyme) that serves as an active site to catalyze a reaction? F. What would happen if aspartic acid were replaced with tryptophan in a non-active site?
9. A) Please write down the names of the following protein folds. A B C B) Which one(s) is made of more than one polypeptide? D E 000 C) Give an example of a protein containing the motif in C and explain how the structure of this motif facilitates function. 10. What is Levinthal's paradox? Describe the paradox and explain the conclusion to which it led.
36. Which of the following is true? A. All proteins possess primary, secondary, tertiary and quaternary structure B. Proline is the least common amino acid in alpha-helices due to its inability to fully participate in intrahelical hydrogen bonding C. Once denatured, proteins cannot be renatured or restored to the native state D. The subunits of oligomeric proteins are always identical 37.The pka's of the side chain group and the alpha-carboxyl group of glutamate are 4.1 and 2.1, respectively. Which statement accounts for this difference? A. The side chain has more resonance structures B. The alpha-carboxyl group has less steric hindrance and it is therefore ionized more easily C. The side chain is a different functional group than alpha-carboxyl group D. The alpha-carboxyl group is closer to the alpha-amino group than the side chain is E. None of the above
81. You have used the primary amino acid sequence of a newly identified protein (of unknown function) to make a hydropathy plot. From this plot you believe it might be a transmembrane receptor. This is because the plot tells a. the secondary structure is likely made up of several B sheets. b. the secondary structure is likely made up of a-helices. c. the protein would be readily hydrolyzed if in an aqueous environment. d. on average, there are a lot of hydrophobic amino acids in the protein. e. there are several hydrophobic areas interspersed with short hydrophilic stretches. you that 82. You are studying a mutant type of garter snake known for its odd slithering movement. You isolated the mutated gene and this morning you just got the results from your DNA sequencing. What would be your first step towards determining the potential function of the protein encoded by this gene? a. Use X-ray crystallography to determine the tertiary structure of the protein. b. Use computer programs that…
4) For various amino acid pairs (for example: F to A, E to R, D to N, V to L, S to W), ask yourself: a) Based on what you know about the chemical properties of the side chains, what effect would you expect on the stability of the protein if you mutated one residue of the pair into the other in the interior of the protein? What forces might have an impact on this change (ie: what types of interactions would you expect that amino acid to be involved in?) How would your answer change if the amino acid were located on the surface of the protein? b) c)
Which of the following statements are correct about the molten globular state of protein folding (select all that appy)? A. May be short-lived or long-lived intermediate in protein folding B. Contains substantial levels of secondary structure C. Has loose packing of hydrophobic core D. Larger radius of gyration than dentaured state E. Is a more compact state than the native confomation
3b) Both a-helical 2° structure and b-pleated sheet 2° structure result from the same type of interaction; briefly explain in your own words why you might observe an a-helix in one region of a protein and a b-pleated sheet in another region of the same protein.
1. Determine the molecular properties of amino acids; - what happens to the protein folding pattern when amino acid composition and solvents are changed such as water and oil 2. Explain the chemical basis of protein folding; and, - What influences protein folding? (Ph, temp, presence of enzymes, chemical reactions) 3. Compare the molecular property of amino acids and their roles in protein folding. (tpsa, logP, molecular refractivity, geometric distance, HBA1) Hydrophilic acids Arginine Asparagine Aspartic Acid Cysteine Glutamic acid Glutamine Glycine Histidine Lysine Serine Threonine hydrophobic acids Alanine Isoleucine Leucine Methionine Phenylalanine Proline Tryptophan Tyrosine Valine
40.What would you expect about the formation of an alpha-helix for a segment of a protein chain that contains lysine approximately every four residue with all other residues being mostly hydrophobic? A. Helix formation would be favored at low pH B. Helix formation would be favored at high pH C. Helix formation would be favored at neutral pH D. Helix formation would never occur regardless of pH
9. Which of the following statements is TRUE regarding the pressure denaturation of proteins? a. High pressure drives protein conformational equilibria towards the physically larger state. b. Pressure drives the noncovalent aggregation of proteins. c. With increasing pressure, denaturation is preceded by water invasion into internal voids. d. Pressure denaturation is easily achieved near atmospheric pressure. e. Pressure denaturation is mechanistically similar to thermal denaturation.
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).
Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala

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