Super urgent: Explain why Histidine does not act as a basic acidic amino in general acid-base catalysis of lysozyme, which is at pH near 4.5? (His pka = 6.0)
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Super urgent: Explain why Histidine does not act as a basic acidic amino in general acid-base catalysis of lysozyme, which is at pH near 4.5? (His pka = 6.0)
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- 1. pH Effects a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52 and Glu35, are critical for catalytic activity. If we assume normal side chain pKa values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of enzyme molecules will have both Asp52 and Glu35 in the correct ionization state at pH 5.0 (the pH optimum for lysozyme)? b. Are the traditional pKa values likely to be correct within the protein? What pKa changes might be present within lysozyme?Help pleaseNeed help, please. Draw an oxygen binding curve of Hb at a pH of 7.4 and another curve where all 2,3 BPG has been removed Draw an oxygen binding curve of Hb at a pH of 7.4 and another at pH. Draw an oxygen binding curve of Hb at a pH of 7.4 and another with a mutant Hb in which the predominant form of the protein is monomeric
- d. Which of the substrates is likely to have a higher Vmax. What is your reasoning? e. Can you propose a molecule that might act as an inhibitor to this reaction? Explain your reasoning.Please ASAP. Thank you. Explain these results in short answer form. Why was the slope zero for blank solution? What was the optimal concentration for peroxidase activity? Do these values make sense?Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?
- . The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAGwhat is lactose intolerance ? describe the molecular life cycle for this disease. also describe how it occurs in a molecular level detailed mechanism. what causes this disease and how it develops ? provide detailed biochemical phenomena and life cycle for Lactose Intolerance condition.Protein purification table: A 50 ml crude skeletal muscle extract contains 32mg of protein per ml. Ten ul of the extract catalyzes a reaction at a rate of 0.14 µmol product per minute. The extract was fractionated by ammonium sulfate precipitation, and the fraction precipitating between 20% and 40% saturation was dissolved in 10ml. The solution contains 50mg/ml protein. Ten ul of this purified fraction catalyzes the reaction at a rate of 0.65 µmol/min (a) What is the degree of purification (fold purification)? (b) What is the percent yield of the enzyme recovered in the purification?
- . The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIII don't understand it. Can u help me? Can u help me to explain this to me, please
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