1. In fetal hemoglobin, residue 143 of the beta subunit is a serine rather than the histidine found in adult hemoglobin (see figure on page 9). a) What does this do to the charges in the BPG binding cavity? b) Would you expect this to change the oxygen affinity of fetal hemoglobin, and, if so, in what direction?
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- 2,3-Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?A quantitative amino acid analysis reveals that bovine serum albumin (BSA) contains 0.58% tryptophan (Mr 204) by weight.(a) Calculate the minimum molecular weight of BSA (i.e., assume there is only one Trp residue per protein molecule).(b) Size-exclusion chromatography of BSA gives a molecular weight estimate of 70,000. How many Trp residues are present in a molecule of serum albumin?The figure below shows amino acid interactions between the a /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 Ka of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). to B, V34 8- a, R141 D126 K127 Noncovalent
- 1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…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 Interactions8) A Leu > Ala mutation at a site buried in the core of the enzyme lysozyme ends up being destabilizing. Explain why in terms of AH", AS" (for both the protein and solvent), and AG".
- 2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?Please fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to theIf an extra nucleotide is inserted in the first exon of the beta globin gene, what effect will it have on the amino acid sequence of the globin polypeptides? Will the globin most likely be fully functional, partly functional, or nonfunctional? Why?
- Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobins.b. Are the mildly thalassemic individuals with Leporehemoglobin homozygotes or heterozygotes for theunusual allele?c. Why might these mildly thalassemic people produce less Lepore hemoglobin than normal adulthemoglobin?Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin with two α chains and two β chains,lower levels of an unusual, so-called Leporehemoglobin with two α chains and two chains ineach of which the N-terminal half comes from anormal δ chain and the C-terminal half comesfrom a normal β chain. Certain other individualswho are asymptomatic produce a different, unusualanti-Lepore hemoglobin that contains two α chainsand two chains in which the N-terminal half comesfrom a normal β chain and the C-terminal halfcomes from a normal δ chain.a. Describe an event that could give rise to bothLepore and anti-Lepore hemoglobins(b) Hemoglobin is made of B-globin subunits. The first few mRNA nucleotides for B- globin are given by: (1) (iii) (iv) Write down the DNA sequence that has led to this mRNA and indicate the sense and non-sense strands and the polarity. CE Derive the polypeptide for the sequence using the table of the genetic code (Table Q1 below) and indicate the polarity of the polypeptide chain. First Position (5' end) U A single point mutation in mRNA sequence can cause sickle cell anemia by changing the amino acid Glu to Val. For the given mRNA, indicate the point mutations for the first Glu in the polypeptide sequence that can cause this disease. 5'-AUGGUCCACCUGACUCCUGAGGAGAAG...UGA-3' C The polypeptide of B-globin contains the amino acid Leu. Write down all the anticodons of the tRNA molecules that can potentially code for Val. Indicate the polarity of the anti-codon. A G Table 1. The Codons of the Genetic Code Second Position U Phe Phe Leu Leu Leu Leu Leu Leu Ile Ile Ile Met-Start Val Val Val…