Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 3, Problem 20P
Bovine ribonuclease folds with
Assume
42o C?
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Bovine ribonuclease folds with ΔH° = -280 kJ mol-1 and ΔS° = -0.79 kJ mol-1 K -1. Assume ΔH° and ΔS° are independent of temperature. What fraction of bovine ribonuclease is unfolded at 42 °C?
To approximate the concentration of enzymes in a bacterial cell, assume that the cell contains equal concentrations of 1,000 different enzymes in solution in the cytosol and that each protein has a molecular weight of 100,000. Assume also that the bacterial cell is a cylinder (diameter 1.0 μm, height 2.0 μm), that the cytosol (specific gravity 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this hypothetical cell.
The enzyme lysozyme kills certain bacteria by attacking a
sugar called N-acetylglucosamine (NAG) in their cell walls.
At an enzyme concentration of 2 × 10-6 M, the maximum
rate for substrate (NAG) reaction, found at high substrate
concentration, is 1 × 10-6 mol L¯'s1. The rate is reduced
by a factor of 2 when the substrate concentration is
reduced to 6 x 10-6 M. Determine the Michaelis-Menten
constants Km and k, for lysozyme.
Chapter 3 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 3 - Prob. 1PCh. 3 - Given the following reactions and their...Ch. 3 - The decomposition of crystalline N2O5...Ch. 3 - The oxidation of glucose to CO2 and water is a...Ch. 3 - Prob. 5PCh. 3 - In another key reaction in glycolysis,...Ch. 3 - Assume that some protein molecule, in its folded...Ch. 3 - When a hydrophobic substance like a hydrocarbon is...Ch. 3 - It is observed that as temperature is increased,...Ch. 3 - Suppose a reaction has Ho and So values...
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Undergoing moderate activity, an average person...Ch. 3 - The major difference between a protein molecule in...Ch. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Consider the degradation of glucose to pyruvate by...Ch. 3 - a. Consider the malate dehydrogenase reaction,...Ch. 3 - Bovine ribonuclease folds with Ho = -280 kJmol-1...
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- = A different Fab fragment binds to lysozyme with a dissociation constant of Ka 10-6 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to this Fab? [F] = ab Marrow_forwardThis molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?arrow_forwardGiven the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.arrow_forward
- The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?arrow_forwardRefer to the molecular structure of Molecule 1 (attached image). This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?arrow_forwardThe enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?arrow_forward
- Consider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine residue with a pKa = 6.2 HisB is involved in a stabilizing interaction (His-NH+ ..... -O2C-Glu) with a neighboring glutamic acid residue. For HisB, the Gibbs free energy of deprotonation at pH = 7.0 and T = 293K is ΔG'o = +15 kj mol-1. If you had a solution, at pH = 7.0 and T = 293K, containing this protein: a) What fraction of HisA residues are protonated? b) What fraction of HisB residues are protonated? c) What is the pKa of HisB?arrow_forwardProtein concentration can readily be determined using the Beer-Lambert law: A = e l c where A = absorbance e = molar absorption coefficient (M-1cm-1) l = light path length (cm) c = concentration (M) If the molar absorption coefficient at 280 nm for yeast ADH is 48860 M-1cm-1 and a 10 mL solution of the protein has an absorbance at 280 nm of 0.4 (as measured by a spectrometer with pathlength 1 cm), then what is the concentration of the protein solution (in μM)? i.e. concentration = ______ μM If the molecular weight of the protein is 36849, what is its concentration in mg/mL? i.e. concentration = _______ mg/mL For each part of the question, show your calculations to arrive at your answers.arrow_forwardThe figure shows an example of a thermal denaturation plot. The melting temperature (T) is the midpoint of the temperature range over which denaturation occurs. Percent unfolded 100 80 60 40 20 0 20 Tm E 40 60 Temperature (°C) 80 100 Suppose that a Met residue buried in the folded, hydrophobic core of T4 lysozyme is replaced by mutation with a Lys residue.arrow_forward
- In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?arrow_forwardThe process of a protein folding from an inactive unfolded structure to theactive folded structure can be represented by the following equation: unfolded protein ⇌ folded proteinThe values of ΔH° and ΔS° for the folding of the protein lysozyme are: ΔH ° = -280 kJ/ mol ΔS ° = -790 J/mol • K(a) Calculate the value of ΔG° for the folding of lysozyme at 25 °C.(b) At what temperature would you expect the unfolding of lysozyme tobecome favorable? (c) At what temperature would the ratio of unfolded protein to foldedprotein be 1:5?arrow_forwardWhat would the order of migration be (bottom to top in the gel) in a SDS-PAGE for the following proteins? Concanavalin A (ConA) (a homotetramer of 106 kDa), lysozyme (a monomer of 14.3 kDa) & horse liver alcohol dehydrogenase (ADH) (a homodimer of 80 kDa). a. ADH, ConA, lysozyme b. ConA, ADH, lysozyme c. Lysozyme, ADH, ConA Od. Lysozyme, ConA, ADHarrow_forward
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