### 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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Similar questions

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.
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?
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?
3. A biochemist purified a protein from the bloodstream and determined its molecular weight under several conditions. In 8 M urea, which denatures the polypeptide chain, the molecular weight of the protein was 150,000 Da. She found that under reducing conditions the molecular weight of the protein was 75,000 Da, while under oxidizing conditions the molecular weight of the protein was 150,000 Da. Explain these results.
1. Which of the following are building blocks of proteins? а. amino acids b. monosaccharides с. nucleotides d. peptides fatty acids е. 2. Which of the following statements is true regarding DNA structure? a. DNA is composed of amino acids. b. In DNA, purines pair together and pyrimidines pair together. с. DNA forms a double helix. d. DNA is single-stranded.

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