The α and ẞ subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that arehydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin.Why might this be the case?Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin formsglobular structures.Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunitsthrough van der Waals interactions.Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on othermyoglobin molecules.Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environmentof membranes.

The oxygen binds to protein molecules, which are hemoglobin and myoglobin, but former is classified…

Answered: The α and ẞ subunits of hemoglobin bear…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 15QP

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Similar questions

a. Can a mutation change a proteins tertiary structure without changing its primary structure? b. Can a mutation change a proteins primary structure without affecting its secondary structure?
Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Describe the differences in the four protein structures.
Understanding the Nature of the Ubiquitin-Ubiquitin linkage Draw the structure of the isopeptide bond formed between Gly76of one ubiquitin molecule and Lys48of another ubiquitin molecule.
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
The Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?
If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?
If the coding region of a gene (the exons) contains 2,100 base pairs of DNA, would a missense mutation cause a protein to be shorter, longer, or the same length as the normal 700 amino acid proteins? What would be the effect of a nonsense mutation? A sense mutation?
Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.

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