### Questions on Hemoglobin and Myoglobin Affinities#### Understanding Oxygen Binding Affinities:1. **Question 14: Under normal circumstances:** - **A.** Adult hemoglobin (Hb) binds to oxygen more tightly than myoglobin (Mb) binds. - **B.** Fetal Hb binds oxygen more tightly than adult Hb. - **C.** Adult Hb binds oxygen more tightly than either fetal Hb or Mb binds. - **D.** Mb has the lowest affinity for oxygen of the 3 proteins.#### Protein Structure Analysis:2. **Question 15: Which of the following information belongs to the tertiary structure of the protein?** - **A.** The prosthetic group interacting with the polypeptide through dipole-dipole interactions. - **B.** The side chain of the serine residue at the 57th position interacts with the side chain of the histidine at the 109th position through dipole-dipole interactions. - **C.** Both A and B. - **D.** Neither A nor B.

Hemoglobin and Myoglobin are two proteins that bind oxygen. Hemoglobin binds oxygen in the lungs and…

Answered: 14. Under normal circumstances: A.…

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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10. Which of the following statements is FALSE about proteins? A) The sequence of the atoms in the polypeptide backbone does not vary between different proteins. BYProteins would fold to the most stable conformation with the lowest energy level. C) Misfolded protein can be sent to the proteosome where they will be folded into the correct conformation. DY The three-dimensional structure of a protein is in general determined by the sequence of the amino acids. E) Proteins are linear polymers built of amino acids.
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
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.
9. What technique is used to determine the amino acid sequence of a purified protein? 10. Indicate which of the follow techniques could be used to determine the overall structure of a protein: (Circle all the correct answers) a. Cryo-EM b. High throughput sequencing c. Mass spectrometry d. NMR e. Sanger sequencing f. X-ray crystallography /55 3.
1. To create a fully functional protein, how do their structure help in determining its function? 2. Discuss the reasons why proteins make up the largest percentage of a cell’s weight/mass? 3. How do the advent of bioinformatics help scientists understand the diversity of proteins?
2. Consider the following quaternary cartoon structure below, where each colored shape represents a different subunit. i. ii. iii. How many N-termini are there in this complex? Suppose the blue square and orange triangle subunit are held together by a disulfide bond, sketch below what you would expect to see after the addition of BME. What kind of interactions may be responsible for holding the orange triangle and green circle subunits together? List at least three.
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?
2
29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?
1. What is the possible identity of the AA? a. Aspartic acid b. Lysine c. Alanine d. Proline 2. What is the isoelectric point of AA? 3. What is the pKa responding to the dissociation of the alpha-carboxylic group?
2
6. A quantitative amino acid analysis reveals that bovine serum albumin (BSA) contains 0.58% tryptophan (MW=204) by weight. (a) Calculate the minimum molecular weight of BSA (i.e., assume there is only one Trp residue per protein molecule). (b) Gel filtration of BSA gives a molecular weight estimate of 70,000. How many Trp residues are present in a molecule of serum albumin?

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