300.0 mg conc 0.100 M expID: HM1-001 scale 1) EDCI, HOBT hydrate DIPEA O`HN NH H3CO HN DCM:DMF (1:2) NH 2) workup with 1M HCI (aq.) (add first for 10 min (add second after pre-activation) pre-activation) Boc-Asp(OMe)-OH•DCHA H-Phe-OtBu•HCI Boc-Asp(OMe)-Phe-OtBu molar MW m d V
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- At 25oC the Ksp for PbCl2 is 1.6 × 10–5. Calculate Q for the following: 125.0 mL of 0.0100 M Pb(NO3)2 is mixed with 75.0 mL of 0.0200 M NaCl at 25oCWhich of the following is a spontaneous reaction.? a. Rxn with ΔH =- 10Kj/mol ΔS= -5J/mol T= 300K b. NaCl +H20 -> NaOH + HCl 25C c. H20(l) -> H2O(s) Temp: 25C d. Dissolution of 100g of solid sugar in 100 mL ice tea. Consider following reaction: HgO (s) -> Hg(l) + ½ O2 (g) Delta H = +90.7 kj/mol. What quantity of heat in kj/mol is required to produce one mole HgO? Write your answer without units. Given the following data 2ClF(g) + O2(g) --> Cl2O(g) + F2O (g) Delta H= 167.4 kJ I 2ClF3(g) + 2O2(g) --> Cl2O(g) + 3F2 O (g) Delta H= 341.4 kJ II 2 F2(g) + O2(g) ---> 2F2O (g) Delta H= -43.4 kJ III Calculate the delta H in kJ for below reaction: ClF(g) + F2(g) ---> ClF3(g)The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8
- An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the following data was obtained. [S] in mmoles/L Velocity in mmoles/L/min-1 No inhibitor With inhibitor 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 Calculate the Km of the enzyme in the reaction without inhibitor ________________________ Km’ of the enzyme in the reaction with inhibitor ________________________ Vmax of the uninhibited reaction ________________________ Vmax’ of the inhibited reaction ________________________Ag+ + ligand L --> Ag_ligandL_Complex K_bind = ??? The virtual lab below contains a 1.00M flask of 'Ligand L' along with a bottle of solid silver chloride. Perform an experiment in the virtual lab to determine the binding constant for this ligand (K_bind for the above reaction). ou will need to use your knowldedge of solubility to determine tthe binding constant. The Ksp for Silver Chloride is: 1.830e-10. Agcl 0.971351 What is the binding constant for this ligand (Please use three significant figures for your answer)The Ksp of Al(OH)3 (MM: 78) is 1.90 xx 10^(-33). a) What is the solubility of Al(OH)3 in g/L?
- 18. Jet is an undergraduate chemistry student, he’s out in the laboratory trying to determine the volatile organic compounds as well as overall protein content of the leaf and stem of a malunggay (Moringa oleifera). He subjected the leaf and stem in a separate digestion reaction (treatment of sulfuric acid), afterwards he subjected the products to high temperature induction to get a dry ash like substance. Which type/s of chemical analysis did Jet employ to reach his objective?I. Qualitative AnalysisII. Quantitative Analysis III. Instrumental Chemical AnalysisIV. Wet Chemical AnalysisA. II & IV onlyB. I & IV onlyC. I, II & IV onlyD. I, II, III, IVFor the reduction 2FeCl3 + SnCl2 =====➔ 2 FeCl2 + SnCl4 in aqueous solution the following data were obtained at 25oC t(min) 1 3 7 11 40 Y 0.01434 0.02664 0.03612 0.04102 0.05058 Where y is the amount of FeCl3 reacted in moles per liter. The initial concentrations of SnCl3 and FeCl3 were respectively, 0.03125, 0.0625 moles/L. a.)Show that the reaction is third order (derive the rate law), and b.) calculate the average specific rate constant.For the reaction 2Na (g) Na2 (g) the following values of K have been determined (C. T. Ewinget al., J. Chem. Phys. 1967, 71, 473):T (K) K900 1.321000 0.471100 0.211200 0.10From these data, estimate rxnH° for the reaction.
- Aleks data for PbCO3 is 7.40 x 10^-14.a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 micrograms/micromole; 8 micrograms of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?The catalytic efficiency of many enzymes depends on pH. Chymotrypsinshows a maximum value of kcat/KM at pH 8. Detailed analysis shows thatkcat increases rapidly between pH 6 and 7 and remains constant at higherpH. KM also increases rapidly between pH 8 and 10. Suggest explanationsfor these observations.