Calculate the standard reduction of 3-phosphoglycerate using val ues from your book, and compare the reduction potential to others tabulated in the book.
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- Assume that the reaction Arabinose +Pi Arabinose-6-P has a delta G of +16.1 kJ/mol and the reaction XTP XDP + Pi has a delta G of -24.7 kJ/mol. Calculate the delta G for the combined reaction Arabinose + XTP Arabinose-6-P + ADP, in kJ/mol to four significant figures.Calculate the ratio of [fumarate] to [succinate] under cellular conditions at 37°C.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.
- Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/molProline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?Tirofiban (C22H36N₂O5S MWt = 440.6) is present as tirofiban HCI monohydrate MWt=495.1) at 0.281 mg/mL in a concentrated solution. (C22H36N2O5S.HCI.H₂O A solution for infusion is prepared by extracting 50 mL from a 250 mL bag of 5% glucose s and adding 50 mL of concentrated solution. Sonya who weighs weighs 60 kg requires a tirofiban dose of 0.4 mcg/kg/min for 30 minute- What volume would remain after 30 minutes? Answer: 94.53 mL X The correct answer is: 236 mL
- From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.27. The standard-state free energy of hydrolysis for acetyl phosphate in 1,3-Bisphosphoglycerate is 1,3-Bisphosphoglycerate + H₂O 3-phosphoglycerate + Pi AGI-49.6 kJ/mol. Determine the free energy change for 1,3-Bisphosphoglycerate hydrolysis in a solution of 5.4 mM 3-phosphoglycerate, 0.0054 M inorganic phosphate, and 20 nM 1,3-Bisphosphoglycerate.Methyl-labeled [14C]methionine at a specific activity of 2.0 millicuries per millimole was injected into rats. Six hours later the rats were killed. Phosphatidylcholine was isolated from the liver and found to have a specific activity of 1.5 millicuries per millimole. Calculate the proportions of phosphatidylcholine synthesized by the phosphatidylserine pathway and by the pathway starting from free choline. What further information would you need for your calculated values to reflect the true rates of these processes?
- The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)Quinine ( C20 H24 N2 O2) is the most important alkaloid derived from cinchona bark. It is used as an antimalarial drug. For quinine, pK, = 5.1 and pK, = 9.7 ( pKp = – log Kp). Only 1 g quinine will dissolve in 1920.0 mL of solution. Calculate the pH of a saturated aqueous solution of quinine. Consider only the reaction | Q+ H2O= QH+ + OH- described by pK, where Q = quinine. pH =Calculate the Keq (report up to two decimal places and do not use scientific notation) for the net reaction at 298.15K. (see attached image) Note: R = 1.98 x 10 -3 kcal/mol-K