Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).arrow_forwardLiposomes used in these vaccines contain some cationic lipids, or lipids with a positively charged head group. Explain why this is a sensible strategy for delivering genetic materials (or drugs) to a human cell.arrow_forwardWithin the body, CoQ 10 can be found in an oxidized or reduced form (also known as ubiquinone and ubiquinol). Describe how these structures differ and the biochemical role of coenzyme Q10.arrow_forward
- The mutation in hemoglobin at B82 Lys → Asp results in lowered O,-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site (see Figure 7.29; B82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, sug- gest a rationale for the observed reduction in Oz-binding affinity.arrow_forward. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.arrow_forwardPlease help mearrow_forward
- The formation of “hard” clots by factor XIIIa involves linking lysine and glutamine side chain residues in fibrin. Draw a representation of the cross-linked product of a reaction between these two amino acids.arrow_forwardThe T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.arrow_forwardA very new Hemoglobin variant, called Hb simplex, has just been identified in patients with hypoxia (i.e. patients for whom the oxygenation of organs is not properly accomplished). However, this variant is able to bind dioxygen with a Kd which is significantly lower to that of Hemoglobin from normal patients. This effect has been associated with the substitution of a Lys by a Met at two distinct sites of the b subunit of Hemoglobin : one site close to the N-terminus, and the other site close to the C-terminus of the polypeptide chain. Most importantly, these 2 sites are known to be involved in the maintain of the physical interactions between the subunits a and b in Hemoglobin. 1) The aforementioned Hb simplex mutations lead to a loss of physical interactions between the subunits a and b. What type(s) of chemical bonds between the 2 subunits (i.e. covalent, electrostatic, ion-dipole, dipole-dipole, van der waals) would you hypothesize to be affected by these mutations? explain. 2)…arrow_forward
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