1. What is hemoglobinopathy? What is sickle-cell anemia? Explain the concept relating to protein structure. 2. How does the oxygen-carrying functions of myoglobin differ from that of hemoglobin?
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1. What is hemoglobinopathy? What is sickle-cell anemia? Explain the concept relating to protein structure.
2. How does the oxygen-carrying functions of myoglobin differ from that of hemoglobin?
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- 29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?What exactly happens in hemoglobinopathy and what is sickle cell anemia? How are these related to the structure of proteins in our body?26. Describe the structure of hemoglobin. 1+ Hemoglobin Location of Hb # of protein chains in 1 molecule of Hb Name of protein in Hb? I # of heme groups in 1 molecule of Hb # of iron atoms in 1 molecule of Hb # of O₂ molecules 1 molecule of HB can transport #of O₂ molecules 6 molecules of Hb can transport Color of blood when O₂ bound to Hb Color of blood when no O₂ bound to Hb Part of Hb that binds to 0₂ Part of Hb that binds to CO₂ Part of Hb that binds to H* ions Which type of Hb (adult or fetal) has a greater affinity (attraction to O2)? What hemoglobin A1C levels measure Description Four protein chains Four heme groups Four iron atoms Four oxygen molecules Bright red Dark red Iron atom 4 iron atoms Fetal HB What % of the patients Hemoglobin is coated with Sugar (glycated)
- Hemoglobin is a protein that carries oxygen in the blood. It is formed by two alpha subunits and two beta subunits. Which of the following statements about hemoglobin is INCORRECT? a. The structure of hemoglobin is stabilized by hydrogen bonding, hydrophobic packing and hydrophilic exposure. b. Hemoglobin has primary, secondary and tertiary structures, but no quaternary structure. c. Hemoglobin is a hetero-tetramer as it is formed by four subunits. d. It is an oligomer.Hemoglobin is composed of which two types of polypeptide chains, alpha?Give 2 structural features in each of the given proteins below that make them perform their biological roles effectively (structural features that directly make them effective in their respective biological roles). Explain how each structural feature directly contributes to proteins’ biological roles. hemoglobin immunoglobulin
- 3. Draw the chemical structure of cholesterol and state its functions 4. Explain in detail the structural organization of proteins 5. The human hemoglobin is a tetrameric protein of about 64.5 KDa, consisting of two a- chains and two B-chains tightly bound. a) Calculate the number of amino acids present in the a-chains b) What is the length of each B-chain? c) What is the sum of the length of the two a-chains? d) Find the length of the tetrameric protein hemoglobin assuming its all an alpha helical structure. 6. Study the polypeptide structure sequence of a B-strand shown below Lys-Gly-Asp-Trp-Ser-Glu a) Draw the chemical structure of the polypeptide. Indicate on the structure the backbone and peptide bonds b) Calculate the weight of the protein in KDa c) Calculate the length of the protein.68. A protein contained in red blood cells is called _________ and it is made up of ________ polypeptide(s). hemoglobin, 3 hemoglobin, 4 myoglobin, 4 ferroglobin, 41.Globular proteins fold up in compact, spherical structures that have uneven surfaces. They tend to form multi-subunit complexes, which also have a rounded shape. Fibrous proteins, on the other hand, span relative large distances within the cell and in the extracellular space. Which of the proteins below are fibrous proteins? a. collagen, keratin b. tubulin and actin monomers c. elastase, pepsin d. hemoglobin and myoglobin 2. Which of the following statements is correct regarding oxidoreductase enzymes? a. NADH + H+/NAD+ are involved in catabolism and NADPH + H+/NADP+ participate in anabolism. b. The oxidation of the reduced member of a redox pair is associated to a ΔΔG < 0. c. The reduction of the oxidized member of a redox pair is associated to a ΔΔG > 0 d. All of the above e. None of the above 3.Which of the following statements is incorrect? a. We only need to consume vitamins in small amounts b. Vitamins are precursors to…
- 1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.1. a. Explain why the melting point of palmitic acid (16 carbons, no double bonds) is slightly lower thanthat of stearic acid (18 carbons, no double bonds). Explain why the melting point of oleic acid (18carbons, one double bond) is lower than that of stearic acid b. A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen. Luckily, metabolically active tissues have some tricks for encouraging hemoglobin to give up oxygen. Name and explain the "trick" depicted by images below. In your answer, be certain to explain the effect on hemoglobin structure. 1.0 a2 Lys 40 pH 7.6 Y 0.5- `pH 7.4 C terminus pH 7.2 Added + proton B, His 146 B, Asp 94 6. 10 po2 (kPa) Figure 7-19 Biochemistry, Sinth Edition 2ea/ H freenard Camny Figures16 Lhninge Principies of iecheminy Seventh dton 2017W.H Feenan and Company