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Problem 6 A hemoglobin tetramer with two a-subunits (143 amino acid residues each) and two ẞ-subunits (147 amino acid residues each) was isolated from a lungfish (shown below amino acids 1-74 of each shown above and 75-end shown below). The a- and ẞ- chains can be shown to be homologous with about 51 identical residues when two gaps are introduced. Of the five sections underlined, four have at least 35% homology between the a- and ẞ- chains while one has very little homology. For parts a-d, choose from the five underlined sections of the B-chain: a MRFSQDDEVLIKEAWGLLHQIPNAGGEALARMFSCYPGTKSYFPHFGHDFSANNEKVKHHGKKVVDAIGQGVQH ẞ VHWEDAEKQYIVSVFSKIDVDHVGANTLERVLIVFPWTKRYFNSFGDLSSPGAIKHNNKVSAHGRKVLAAIIEC a LHDLSSCLHTLSEKHARELMVDPCNFQYLIEAIMTTIAAHYGEKFTPEINCAAEKCLGQIVHVLISLYR ẞ TRHFGNIKGHLANLSHLHSEKLHVDPHNFRVLGQCLRIELAAALGFKEFTPERNAYFQKFMDVISHSLGREYH a) Choose a section that would be expected to participate in the coordination of the heme iron and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) β b) Choose a section that would be expected to participate in the allosteric binding site and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) α В c) Choose a section (not the same as your a or b choices) that would be expected to exist in a predominantly α-helical section of the tertiary structure and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. В d) Which of the sequences that you chose in (a), (b) and (c) has the least sequence homology? Explain how this relates to the function of this section of the protein.

Problem 6 A hemoglobin tetramer with two a-subunits (143 amino acid residues each) and two ẞ-subunits (147 amino acid residues each) was isolated from a lungfish (shown below amino acids 1-74 of each shown above and 75-end shown below). The a- and ẞ- chains can be shown to be homologous with about 51 identical residues when two gaps are introduced. Of the five sections underlined, four have at least 35% homology between the a- and ẞ- chains while one has very little homology. For parts a-d, choose from the five underlined sections of the B-chain: a MRFSQDDEVLIKEAWGLLHQIPNAGGEALARMFSCYPGTKSYFPHFGHDFSANNEKVKHHGKKVVDAIGQGVQH ẞ VHWEDAEKQYIVSVFSKIDVDHVGANTLERVLIVFPWTKRYFNSFGDLSSPGAIKHNNKVSAHGRKVLAAIIEC a LHDLSSCLHTLSEKHARELMVDPCNFQYLIEAIMTTIAAHYGEKFTPEINCAAEKCLGQIVHVLISLYR ẞ TRHFGNIKGHLANLSHLHSEKLHVDPHNFRVLGQCLRIELAAALGFKEFTPERNAYFQKFMDVISHSLGREYH a) Choose a section that would be expected to participate in the coordination of the heme iron and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) β b) Choose a section that would be expected to participate in the allosteric binding site and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) α В c) Choose a section (not the same as your a or b choices) that would be expected to exist in a predominantly α-helical section of the tertiary structure and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. В d) Which of the sequences that you chose in (a), (b) and (c) has the least sequence homology? Explain how this relates to the function of this section of the protein.

Biochemistry
Biochemistry
9th Edition
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Chapter3: Amino Acids And Peptides
Section: Chapter Questions
Problem 8RE: MATHEMATICAL Draw structures of the following amino acids, indicating the charged form that exists...
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help me with a, b, c, d please

Problem 6 A hemoglobin tetramer with two a-subunits (143 amino acid residues each) and two ẞ-subunits (147 amino acid residues each) was isolated from a lungfish (shown below amino acids 1-74 of each shown above and 75-end shown below). The a- and ẞ- chains can be shown to be homologous with about 51 identical residues when two gaps are introduced. Of the five sections underlined, four have at least 35% homology between the a- and ẞ- chains while one has very little homology. For parts a-d, choose from the five underlined sections of the B-chain: a MRFSQDDEVLIKEAWGLLHQIPNAGGEALARMFSCYPGTKSYFPHFGHDFSANNEKVKHHGKKVVDAIGQGVQH ẞ VHWEDAEKQYIVSVFSKIDVDHVGANTLERVLIVFPWTKRYFNSFGDLSSPGAIKHNNKVSAHGRKVLAAIIEC a LHDLSSCLHTLSEKHARELMVDPCNFQYLIEAIMTTIAAHYGEKFTPEINCAAEKCLGQIVHVLISLYR ẞ TRHFGNIKGHLANLSHLHSEKLHVDPHNFRVLGQCLRIELAAALGFKEFTPERNAYFQKFMDVISHSLGREYH a) Choose a section that would be expected to participate in the coordination of the heme iron and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) β b) Choose a section that would be expected to participate in the allosteric binding site and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) α В c) Choose a section (not the same as your a or b choices) that would be expected to exist in a predominantly α-helical section of the tertiary structure and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. В d) Which of the sequences that you chose in (a), (b) and (c) has the least sequence homology? Explain how this relates to the function of this section of the protein.
Transcribed Image Text:Problem 6 A hemoglobin tetramer with two a-subunits (143 amino acid residues each) and two ẞ-subunits (147 amino acid residues each) was isolated from a lungfish (shown below amino acids 1-74 of each shown above and 75-end shown below). The a- and ẞ- chains can be shown to be homologous with about 51 identical residues when two gaps are introduced. Of the five sections underlined, four have at least 35% homology between the a- and ẞ- chains while one has very little homology. For parts a-d, choose from the five underlined sections of the B-chain: a MRFSQDDEVLIKEAWGLLHQIPNAGGEALARMFSCYPGTKSYFPHFGHDFSANNEKVKHHGKKVVDAIGQGVQH ẞ VHWEDAEKQYIVSVFSKIDVDHVGANTLERVLIVFPWTKRYFNSFGDLSSPGAIKHNNKVSAHGRKVLAAIIEC a LHDLSSCLHTLSEKHARELMVDPCNFQYLIEAIMTTIAAHYGEKFTPEINCAAEKCLGQIVHVLISLYR ẞ TRHFGNIKGHLANLSHLHSEKLHVDPHNFRVLGQCLRIELAAALGFKEFTPERNAYFQKFMDVISHSLGREYH a) Choose a section that would be expected to participate in the coordination of the heme iron and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) β b) Choose a section that would be expected to participate in the allosteric binding site and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. (Explain your choice briefly.) α В c) Choose a section (not the same as your a or b choices) that would be expected to exist in a predominantly α-helical section of the tertiary structure and give the corresponding sequence of the a-chain that would exist in the same positions in the tertiary structure. В d) Which of the sequences that you chose in (a), (b) and (c) has the least sequence homology? Explain how this relates to the function of this section of the protein.
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