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 2P
Bovine pancreatic trypsin inhibitor (BPTI; Figure 6.25) contains six cysteine residues that form three disulfide bonds in the native structure of BPTI. Suppose BPTI is reduced and unfolded urea (as illustrated for RNase A in Figure 6.22). If the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?
Figure 6.22 The denaturation and refolding of ribonuclease A.
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Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.
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Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.
Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.
do not coy from other answers here
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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- An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?arrow_forwardSome of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.arrow_forwardThe active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state(protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme shown below?arrow_forward
- Tryptophan is not classified as a basic amino acid even though it has aheterocycle containing a nitrogen atom. Why is the N atom in the fivemembered ring of tryptophan not readily protonated by acid?arrow_forwardThe enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?arrow_forward(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein. (iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond. (v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes. Answer (iii) to (v) please.arrow_forward
- The subunits of hemoglobin and myoglobin share structural similarities. Some residues are hydrophilic in hemoglobin but are hydrophilic in myoglobin. Give an explanation as to why this may be the case.arrow_forwardThe active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?arrow_forwardDraw the structure of the α-keto acid formed by the transamination of each amino acid: (a) tyrosine; (b) asparagine.arrow_forward
- The enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found in bacterial cell walls. The active site of lysozyme contains two amino acid residues essential for catalysis: E35 and D52. Which of the following statements about lysozyme is true? More than one may apply The graph shows the pH-activity profile of lysozyme. 100 50 4. 6. 8. 10 pH Residue E35 exhibits general base catalysis O The pKa of E35 is approximately 4.3 O The pKa of D52 is approximately 4.5 O The optimal activity of lysozyme is approximately 5.2 Residue E35 exhibits covalent catalysis The pka of E35 is approximately 6.1 The pka of D52 is approximately 3.7 Activity (% of maximal)arrow_forwardOne of the reasons for oxidizing the disulfide bonds in RNase A before removing the urea in the Anfinsen experiment was to demonstrate that ... Urea promotes disulfide bond exchange O Incorrectly-folded proteins lose their enzymatic activity. Urea prevents disulfide bond formation. Urea forms thio-esters with reduced cysteines at pH 8.2 Disulfide bonds are required for enzyme activity.arrow_forwardCeruloplasmin is a blue-colored monomeric oxidase found in mamma- lian blood plasma. It contains multiple copper atoms per mole- cule. A ribbon representation of its three-dimensional shape is shown below: a) b) c) Identify any cofactor(s) which ceruloplasmin may possess. How do you know? Does ceruloplasmin act as an enzyme ? Describe the secondary, tertiary and quaternary structures of ceruloplasmin.arrow_forward
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