4. You are to choose the members of an expedition that will climb several high mountains.Each applicant for one of the positions is a heterozygote for an abnormal hemoglobin:Person A: Hb Albany: a methionine has been substituted for Lys 82 in the B-subunit.Person B: Hb Cowtown: a leucine has been substituted for His 146 in the B-subunit.Person C: Hb Flagstaff: an isoleucine has been substituted for Val 1 in the B-subunit. and the KİNG exercises. Assuming that each of these candidates is equal in ability at lowaltitude, which one would you choose for the expedition? To answer this question, determinehow the substituted amino acid affects the structure and function of each abnormalhemoglobin, and describe the physiological effect. Focus on the stabilization of the T versusR state of hemoglobin, and the consequent physiological changes that might occur at highaltitude. Keep your answers brief.Person APerson BPerson C

Hemoglobin abnormalities are referred to as the type of blood disorders that have a major impact on…

Answered: 4. You are to choose the members of an…

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter16: Human Genetics And The Human Genome

Section: Chapter Questions

Problem 6TYU

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1. Hemoglobin researchers have discovered more than 500 naturally occurring hemoglobin mutations. The majority of these results from single amino acid changes. Some of these mutations result in clinical illness or symptoms, but many show no outward effects. Some examples are: HbS (sickle cell Hb)-substitutes Val for Glu on the surface Hb Cowtown - eliminates an ion pair used in T-state stabilization Hb Memphis - surface uncharged polar aa for another of similar size on the surface Hb Bibba-substitutes a Pro for a Leu in an α-helix Hb Milwaukee - substitutes a Glu for a Val Hb Providence- substitutes a Asn for a Lys that normally projects into the central cavity Hb Philly - substitutes a Phe for a Tyr, disrupting hydrogen bonding at the aß 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 pl values different from that of HbA c) The variant(s) most likely to show…
1. How many different tripeptides are possible? How many carboxyl terminals of polypeptide chains are present in a molecule of hemoglobin? 2. You have isolated a pentapeptide composed of four glycine residues and one lysine residue that resides at the C-terminus of the peptide. Using the information provided in the legend of Figure 2.27, if the pK of the side chain of lysine is 10 and the pK of the terminal carboxyl group is 4, what is the structure of the peptide at pH 7? At pH 12? 3. The side chains of glutamic acid (pK 4.3) and arginine (pK 12.5) can form an ionic bond under certain conditions. Draw the relevant portions of the side chains and indicate whether or not an ionic bond could form at the following: (a) pH 4; (b) pH 7; (c) pH 12; (d) pH 13.
What impact do mutations in the alpha-chain usually have, if any, on hemoglobin's function? A. T-to-R-state transition B. dimer-dimer stabilization C. Allosteric Regulation D. A & B E. A & C F. A,B, & C
5. All antibodies are proteins. What protein property has favored their use as antibodies in preference to some other type of biomolecule?
4. The strength of ligand-protein binding is a property of the binding site called --------------
3) The ACE2 receptor protein in humans has been getting a lot of press these days, as it apparently serves as a "receptor" for the SARS-CoV-2 coronavirus in addition to its normal functions. This protein has an isoelectric pH of 5.36. Suppose you want to purify this protein to study its properties, with the goal of developing a drug that would block it from binding the virus. Once you have purified the cell surface proteins from your cultured human lung cells away from all the other types of molecules in the cell, and all the cytoplasmic proteins, you might decide to use ion exchange chromatography to separate the ACE2 proteins from other proteins in your sample. If you plan to load your protein mixture onto your ion exchange column in a buffer at pH 7.4 (approximately physiological pH) and you want the ACE2 proteins to bind to the column, should you use a resin with a positive charge or a negative charge? Briefly explain why you chose the resin you selected.
1.Which of the following is not an example of a protein with quaternary structure? a. Calmodulin is a Ca2+-binding protein which is formed by two identical subunits. b. Hemoglobin in adult humans has the composition αα2ββ2. c. The photosynthetic enzyme Rubisco is composed of 8 L subunits and 8 S subunits. d. Myoglobin, an oxygen-binding protein in muscle, consists of a single subunit. e. South American rattlesnake toxin (crotoxin) is a phospholipase A enzyme with two different subunits. 2.Complete the sentence with the best option provided below. The secondary structures of a protein are the a. chemical modifications of amino acid side chains. b. temporary, unstable protein folding conformations. c. regular, repeated folds present in a lowest energy conformation. d. interactions between polar amino acid side chains.
1. Below is the base sequence of protein for normal hemoglobin and the base sequence for the sickle cell hemoglobin:Normal: GGG CTT CTT TTTSickle: GGG CAT CTT TTTa. Transcribe and translate the normal and sickle cell DNA. b. Identify this as a point or frameshift mutation. Explain. c. If the base sequence read GGG CTT CTT AAA instead, would this result in sickle cell hemoglobin? Explain.
Which of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.
12) The tertiary structure of immunoglobulin G is composed of 12 discrete: A. alpha-helices B. collapsed beta-barrel domains C. parallel beta-sheets D. helix-turn-helix domains
4 How to use the Kd to determine the fraction of both bound proteins? The Kd is 0.05uM. protein 1 has [ ] of 0.03 uM and protein 2 has [ ] of 0.05 uM.
1. Search for the `P06858` a) Give information about the PTM and Processing of this protein. b) Which position has maximum amount of variations? Give details about the variations. (Eg: What kind of variation? Feature ID? Disease association? etc..)

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