Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780321839923
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 6, Problem 9P
a. A protein is found to be a tetramer of identical subunits. Name two symmetries possible for such a molecule. What kinds of interactions (isologous or heterologous) would stabilize each?
b. Suppose a tetramer, like hemoglobin, consists of two each of two types of subunits, a and ß. What is the highest symmetry now possible?
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A protein hypothetically consists of two polypeptide chains with the given sequences in the picture.
Based on the said sequences,
a. Do you think it is possible that interchain disulfide bonds is present in the protein? Explain.
b. Do you think it is possible that intrachain disulfide bonds is present in the protein? Explain.
- (a) A protein is found to be a tetramer of identical subunits. Name
two symmetries possible for such a molecule. What kinds of interac-
tions (isologous or heterologous) would stabilize each?
(b) Suppose a tetramer, like hemoglobin, consists of two each of two
types of chains, a and B. What is the highest symmetry now possible?
A. Where would you expect valine, leucine, and isoleucine to be located in a polypeptide? (Inside or outside)? Explain your answer using the properties of the amino acids listed.
B.How would your answer change, if the amino acids were Lysine and Histidine?
Chapter 6 Solutions
Biochemistry: Concepts and Connections
Ch. 6 - Prob. 1PCh. 6 - Bovine pancreatic trypsin inhibitor (BPTI; Figure...Ch. 6 - A schematic structure of the subunit of...Ch. 6 - In the protein adenylate kinase, the C-terminal...Ch. 6 - Give two reasons to explain why a proline residue...Ch. 6 - Consider a small protein containing 101 amino acid...Ch. 6 - a. Based on a more conservative answer to Problem...Ch. 6 - The following sequence is part of a globular...Ch. 6 - a. A protein is found to be a tetramer of...Ch. 6 - Under physiological conditions, the protein...
Ch. 6 - Theoretical and experimental measurements show...Ch. 6 - The peptide hormone vasopressin is used in the...Ch. 6 - A protein gives under conditions of buffer...Ch. 6 - A protein gives a single band on SDS get...Ch. 6 - It has been postulated that the normal...Ch. 6 - Prob. 16PCh. 6 - Do you expect a Pro Gly mutation in a...Ch. 6 - Rank the following in terms of predicted rates...
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- The given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of different polypeptide chains. Its molecular weight is 200 kDa. Using SDS-PAGE, the protein was characterized and the following profile is the result (attached in the picture). 1: Standard Protein Ladder 2: Protein X solution 3: Protein X solution + β-mercaptoethanol Determine the molecular weights of the three subunits of protein X based on the gel profile. Write the MW of each subunit and explain the obtained answer.arrow_forward3b) 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.arrow_forwardFluorescent proteins like the green fluorescent protein (GFP) found in jellyfish are a class of colorful proteins that shine a particular color when exposed to ultraviolet light. These proteins, despite exhibiting a wide range of diverse colors, have nearly identical secondary structure across organisms and phenotypes. Each GFP-like protein has a few alpha-helices as well as a characteristic beta-barre composed of 11 beta-sheets that shields the inside of the protein from solvent (i.e., water). The GFP like protein shown below is a green fluorescent protein from the great star coral Montastraea cavernosa and contains two alpha-helices in its structure (labeled A and B and colored cyan). A 1. Helix A contains 6 amino acids, including a phenylalanine and an aspartic acid. Which position (1 or 2, colored in red) would you more likely expect aspartic acid to be located? [ Select ] 2. If you were to compare helix A to helix B, would you expect the ratio of polar:non-polar residues to be…arrow_forward
- Fluorescent proteins like the green fluorescent protein (GFP) found in jellyfish are a class of colorful proteins that shine a particular color when exposed to ultraviolet light. These proteins, despite exhibiting a wide range of diverse colors, have nearly identical secondary structure across organisms and phenotypes. Each GFP-like protein has a few alpha-helices as well as a characteristic beta-barrel composed of 11 beta-sheets that shields the inside of the protein from solvent (i.e., water). The GFP- like protein shown below is a green fluorescent protein from the great star coral Montastraea cavernosa and contains two alpha-helices in its structure (labeled A and B and colored cyan). A B 1. Helix A contains 6 amino acids, including a phenylalanine and an aspartic acid. Which position (1 or 2, colored in red) would you more likely expect aspartic acid to be located? [Select] 2. If you were to compare helix A to helix B, would you expect the ratio of polar:non-polar residues to be…arrow_forwardConsider 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?arrow_forwardA protein contains three 60-kD polypeptides and six 20-kD polypeptides. Each 60-kD chain is disulfide bonded to two 20-kD chains. The 100-kD units associate noncovalently to form a protein with a molecular mass of 300 kD. Which of the following is correct? a) PAGE shows one single band b) Molecular masses determined by SDS-PAGE with 2-mercaptoethanol are 20kD and 60 kD c) Molecular mass determined by gel filtration is 300 kD d) All answers are correct e) Molecular mass determined by SDS-PAGE without 2-mercaptoethanol is 100 kD can you explain the steps and calculations to solve this question?arrow_forward
- 3a) The 3° structure of a protein refers to the protein's overall, 3-dimensional shape in space. This will incorporate any 2° structure the protein has, but is predominantly the result of side-group interactions. Name the type of interaction, if any, that you would expect to see under physiological conditions (an aqueous solution at pH 7.0-7.5) between the following pairs of amino acid side groups. Serine and asparagine: Methionine and lysine: Glutamate and aspartic acid: Alanine and phenylalanine:arrow_forwardThe given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of different polypeptide chains. Its molecular weight is 200 kDa. Using SDS-PAGE, the protein was characterized and the following profile is the result (attached in the picture). 1: Standard Protein Ladder 2: Protein X solution 3: Protein X solution + β-mercaptoethanol Based on the given gel profile in the picture, can it be concluded that the solution of Protein X is pure? Explain. can it be concluded that disulfide bonds hold together Protein X's quaternary structure? Explain.arrow_forwardA B 10 Refer to the following figure. How many H-bonds would be present in the four base pairs that are indicated in this sequence: C) 8 D) 12 TT T·* сссG | | | | & E diearrow_forward
- Which of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.arrow_forwardA protein has molecular mass of 200 kDa when measured by gel filtration. When subjected to SDS PAGE with and without 2-mercaptoethanol (2-ME) the gel shown below was obtained. What is the likely subunit composition of this protein and why? a. The protein has 4 subunits, with molecular masses 100, 50, 25, and 25 kDa. 25 kDa subunits are linked to each other via noncovalent interactions. b. The protein has 4 subunits, with molecular masses 100, 50, 25, and 25 kDa. 50 kDa subunit is linked to the one 25 kDa subunit via noncovalent interactions. c. The protein has 3 subunits, with molecular masses 100, 75 and 25 kDa that are linked by noncovalent interactions. d. The protein has 4 subunits, with molecular masses 100, 75, 50 and 25 kDa. The subunits are linked by disulfide bonds. e. The protein has 4 subunits, with molecular masses 100, 50, 25, and 25 kDa. 50 kDa subunit is linked to the one 25 kDa subunit by disulfide bonds.arrow_forwardSuppose you have a mixture of the following proteins protein A: pl = 3.5, mw = 35 kDa protein B: pl = 5.5, mw = 22 kDa protein C: pl = 7.5, mw = 77 kDa protein D: pl = 9.0; mw = 52 kDa. Which protein do you expect to elute last if you perform separation using cation exchange chromatography at pH 7.0? A B Ocarrow_forward
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