Describe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?
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- What are carrier proteins? Explain its types with exampleIs there a difference between the effects of acid concentrations on protein denaturation? Why?There are almost 500 naturally occurring variants of hemoglobin. Most are the result of a single amino acid substitution in a globin polypeptide chain. Some variants produce clinical illness, though not all variants have deleterious effects. A brief sample follows. HbS (sickle-cell Hb): substitutes a Val for a Glu on the surface Hb Cowtown: eliminates an ion pair involved in T-state stabilization Hb Memphis: substitutes one uncharged polar residue for another of similar size on the surface Hb Bibba: substitutes a Pro for a Leu involved in an _ helix Hb Milwaukee: substitutes a Glu for a Val Hb Providence: substitutes an Asn for a Lys that normally projects into the central cavity of the tetramer Hb Philly: substitutes a Phe for a Tyr, disrupting hydrogen bonding at the alß1 interface Explain your choices for each of the following: (a) The Hb variant least likely to cause pathological symptoms. (b) The variant(s) most likely to show pI values different from that of HbA. (c) The…
- The figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent InteractionsExplain why missense changes may or may not affect protein function?Which of the following mutations would most likely keep the transitions of T state to R state in hemoglobin unchanged, or similar to the transitions that occur in the native molecule? The three-letter codes for amino acids are used, and the numbers following the amino acids designate the amino acid position in the protein. By convention, the original, native amino acid is listed fırst, followed by the mutational change. Choose one: O A. Asp94→Ile94 O B. Tyr42→Phe42 O C. Asp94 Glu94 O D. Tyr42-Gly42
- Name and describe the main fuctional macromolecule found in red blood cellsApproximate nH for each protein from its Hill plot. Which proteins exhibits a greater degree of positive cooperativity, normal hemoglobin or the mutant hemoglobin?Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?