16.2 57. Renaturation may be expected in the denatured proteins of which of the following cases?A. Hard-boiled organically farmed eggsB. Heat-straightened curly red-dyed hairC. Hydrochloric acid-washed fungal cellsD. Hydrogen peroxide-treated human blood58. Proteins that get folded into their functional tertiary structures are primarily directed into such conformations by theA. Cellular location in which they are generatedB. Complete total number of the amino acid portionsC. Sequence of their individual amino acid residuesD. Type of covalent interactions between residues

In molecular biology, renaturation refers to the restoration of a protein or nucleic acid (such as…

Answered: 57. Renaturation may be expected in the…

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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1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in zig-zag style, from amino to carboxy terminus, with correct stereochemistry a. Draw the predominant form at pH = 2 b. Draw the predominant form at pH = 5 c. Draw the predominant form at pH = 7 d. Draw the predominant form at pH = 12
The structures of the amino acids lysine and aspartic acid are shown: H₂ H OH CH₂ CH₂ CH₂ CH₂ NH₂ Lysine H H H N-C-C CH₂ C OH O НО Aspartic Acid The tertiary structure of a given protein contains an interaction between aspartic acid and lysine. a. Explain how the structure of amino acids determine the function. b. A mutation occurred in DNA of a globular enzyme. If the lysine amino acids were found within the active site of the enzyme, describe the effect this change is likely to have on enzymatic function. c. If a mutation in the DNA of a globular enzyme changed all of the lysine amino acids to aspartic acid, predict how the relative position of the amino acid in the tertiary structure of the protein would be affected when the protein is placed in an aqueous solution. d. Justify your prediction by providing evidence that supports your claim.
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.
Patients suffering from sickle cell anemia have a mutation in the gene that codes for one of the hemoglobin chains, in which a single glutamate is replaced by a valine. Propose an explanation for why this substitution has such a striking effect on protein structure and function with explanation. Suggest two other amino acids that would be less likely to cause such serious impairment of hemoglobin function if each was substituted for glutamate. Briefly explain your answer.
1) If a mutation caused an alanine to turn in glycine, what kind of effect do you think that would have on the protein structure? Explain your reasoning. 2) If a mutation caused an alanine to turn into a glutamine, what effect do you think that would have on a protein? Explain your reasoning.
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
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)
1. Consider the peptides P-A-I-G-E and M-A-T-T. a. Draw the structure of each peptide at a pH of 7.0 b. Draw the structure of each peptide at a pH of 12.0 c. Calculate the pl of both peptides. Based on your answer, do you think these two peptides can be separated using ion exchange chromatography at a pH of 5? Explain.
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
A. One example of conjugated protein that contains the following Prosthetic groups: a. Iron Protein class, Example, b. Lipids Protein class, Example, c. Phosphate group Protein class, Example, d. Carbohydrate Protein class, Example, е. Heme Protein class, Example,
Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins. (a) What level is shown by doublestranded DNA? (b) What level is shown by tRNA? (c) What level is shown by mRNA?

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