Compare and contrast the entropy changes of the dissolution of the following two amino acids isoleucine and glutamate (in water)
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Compare and contrast the entropy changes of the dissolution of the following two amino
acids isoleucine and glutamate (in water)
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- The formation of maltose, a disaccharide, from two glucose molecules, is not energetically favorable. However, if this reaction is coupled with the hydrolysis of ATP, the reaction occurs more favorably. Maltose + H2O = 2 Glucose , ΔG'o = -15.5 KJ/mol or -3.7 kcal/mol a. Determine if the coupled reaction will occur spontaneously at standard state through calculating the Gibbs Free Energy of Reaction. b. Calculate the equilibrium constant for each individual reaction, and for the coupled reaction (using free energy of reaction). Show that the equilibrium constant for the coupled reaction equals the equilibrium constants for the individual reactions multiplied together. c. If the reaction medium contains the following chemical species at their given concentrations (298 K and 1.0 atm, pH = 7.0), will the reaction proceed in the forward or the reverse direction? [Maltose] = [Glucose] = 10.0 mM; [ATP] = 5.0 mM; [ADP] = [Pi] = 20 mMThe equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]Discuss the behavior of enzymes as described by the Michaelis-Menten Equation
- The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.Produce a reading log for the sections in your text that discuss the Michaelis-Menten equation, including kat Focus on the derivation of the Michaelis-Menten equation. List and explain the assumptions underlying the Michalis-Menten equation. Provide definitions for each term. What is equal at equilibrium? What is the general expression Keg (the equilibrium constant) in terms of product and reactant concentra- tion?Lactic Acid (shown below) is built up in the body during intense workouts as a result of glycolysis. Please denote if the compound is R or S. Also, explain at least two intermolecular forces it would exhibit. Would you expect this compound to be soluble in water?
- The standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alanineDerive an Equation that explains the realtionship between kE and kN with respect to the equilibrium constants provided in the reaction scheme provided below. Assume that the enzyme must bind with A before it binds with B. The two reactions are related by the following reaction scheme:provided below.Determine the values of KM and Vmax for the decarboxylation of a β-keto acid given the following data.
- The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.Mixtures of amino acids can be analyzed by first separating the mixture into its components through ionexchange chromatography. Amino acids placed on a cation-exchange resin containing sulfonate ( -SO3-) groups flow down the column at different rates because of two factors that influence their movement: (1) ionic attraction between the sulfonate residues on the column and positively charged functional groups on the amino acids, and (2) aggregation of nonpolar amino acid side chains with the hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine which will be eluted first from the cation-exchange column by a pH 7.0 buffer. (a) Aspartate and lysine (b) Arginine and methionine(c) Glutamate and valine (d) Glycine and leucine (e) Serine and alanineGastric juice (pH 1.5) is produced by pumping HCl from blood plasma (pH 7.4) into the stomach. Calculate the amount of free energy required to concentrate the H+ in 1 L of gastric juice at 37 °C. Under cellular conditions,how many moles of ATP must be hydrolyzed to provide this amount of free energy? The free-energy change for ATP hydrolysis under cellular conditions is about −58 kJ/mol . Ignore the effects of the transmembrane electrical potential.