![Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)](https://www.bartleby.com/isbn_cover_images/9780134261256/9780134261256_largeCoverImage.gif)
Concept explainers
Interpretation:
Amino acid that can replace glutamate that causes least disruption to the hemoglobin structure has to be identified.
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino
Sickle-cell anemia is a hereditary disease caused by genetic difference that replaces one amino acid (glutamate) with another in each of the two polypeptide chains of the hemoglobin.
![Check Mark](/static/check-mark.png)
Want to see the full answer?
Check out a sample textbook solution![Blurred answer](/static/blurred-answer.jpg)
Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
- The affinity of hemoglobin for oxygen varies according to the pH of the plasma. In fact, the warmer and more acidic your blood is, the more likely it is that hemoglobin will let go of oxygen. Explain, in terms of the secondary and tertiary structure of protein why this would be so.arrow_forwardHeparin, a highly negatively charged glycosaminoglycan, is used clinically as an anticoagulant. It acts by binding several plasma proteins, including antithrombin III, an inhibitor of blood clotting. The 1:1 binding of heparin to antithrombin III seems to cause a conformational change in the protein thatgreatly increases its ability to inhibit clotting. What amino acid residues of antithrombin III are likely to interact with heparin?arrow_forwardWhich intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.arrow_forward
- 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 herearrow_forwardGlobular 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. please do not copy from other answers herearrow_forwardIn the molecule of oligomeric protein there are 19 lysine residues. 12 of them may be easily acetylated with anhydrides of dicarbon acids (it react with NH2-groups). The acetylation of extra two residues of lysine will dissociate the protein to the subunits. The rest 5 lysine residues may be modified only after denaturation of the protein. Suggest, how many lysine residues are: a) on a surface of protein globule; b) inside globule: c) in a site which is responsible for the contact within subunitsarrow_forward
- Commercially available high-energy formulas for premature infants are rich in triacylglycerols containing short- and medium-chain fatty acids esterified at the sn-3 position. Why?arrow_forwardA cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.arrow_forwardThe pKa of an acid depends partly on its environment. Predict the effect of each of the following environmental changes on the pKa of a glutamic acid side chain. (a) A lysine side chain is brought into proximity. (b) The terminal carboxyl group of the protein is brought into proximity. (c) The glutamic acid side chain is shifted from the outside of the protein to a nonpolar site insidearrow_forward
- The a and ß subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that are hydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin. Why might this be the case? O Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other myoglobin molecules. O Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through van der Waals interactions. Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms globular structures. Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.arrow_forwardMyoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.arrow_forwardHemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. 1. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer. This process is not 100% efficient, so we may have leftovers of dimers and monomers. In the graph given, can we label the peaks given as a tetramer, dimer, or monomer?arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
![Text book image](https://www.bartleby.com/isbn_cover_images/9781319114671/9781319114671_smallCoverImage.jpg)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781464126116/9781464126116_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781118918401/9781118918401_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305961135/9781305961135_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305577206/9781305577206_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9780134015187/9780134015187_smallCoverImage.gif)