1. Balance the following equations: a. Al + CuO → Al2O3 + Cu b. Mg + P4 → Mg3P2 c. CaCl2 + AgNO3 → AgCl + Ca(NO3)2 d. BiCl3 + H2O → Bi2O3 + HCl e. SO2(g) + O2(g) + H2O (g) → H2SO4(aq)
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Balance the following equations: a, b, c, d, & e
Please explain thoroughly how and why I would get the balanced numbers properly. If you're going to handwrite it, please write neatly.
Please use vertical, diagonal, and horizontal lines/boxes to determine the balance and cross out the number that is not needed; for example:
C | 8 | 8 |
H | 3 | 5 |
O | 5 | 2 |
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- What are the differences in terms of structure and ligand-binding interactions? What are the functions of each type of GPCR?3. Identify the oxidizing and reducing agent from the following a) MnQ, + 4AF 3Mn+ b) 2CUSO, + S0,+ 2KB1 + 2H02CUBR +2H SO, + K,SO, 2A1 Q: derlined atoms (1x3=3)Which of the following is NOT a REDOX reaction? 2Al(s) + 3CuSO4(aq) → Al2(SO4)3(aq) + 3Cu(s) Cl2(aq) + 2KBr(aq) → Br2(aq) + 2KCl(aq) AgNO3(aq) + KCl(aq) → AgCl(s) + KNO3(aq) Sn(s) + 2HCl(aq) → SnCl2(aq) + H2(g)
- Which of the equations below best represents how excess acid in the blood plasma can be removed in the lungs by breathing? H+ (aq) + 0. 2(g) OH + H₂ CO (aq) OH+ + O (aq) 2(g) → H, CO. H + O₂ (aq) 2(g) 3(aq) 3(aq) → H₂O(g) + CO2(g) + CO2(g) → H₂O H, CO3(aq) → HCO, OH t + HCO3(aq) → H₂ CO3(g) → H₂O(g) (aq) → H, CO3(aq) 3 (aq) + CO2(g) H₂O(g) + CO2(g)B, C The equations are in the other page. Thanks1. Draw an approximate titration curve for lysine, given that its pKa(COOH) = 2.18, its pKa(NH3*) = 8.95, and its pka(R) = 10.53. a. What pH ranges would Lys be a good buffer at? b. What is the pl of Lys? C. Draw the structures of the predominant species in solution at (i) pH 0, (ii) pH 7, (iii) pH 9.5, (iv) pH 12.
- We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…A sample containing Na2CO3 is titrated with HCI. Na2CO3(aq) + 2HCl(aq) →2NaCl(aq) + H2O(l) + CO₂(g) If 0.1800 g sample required 5.64 mL of 0.1082 M HCI, what is the percent Na2CO3 in the sample? O 94.13% O 50.11% O 49.89% O 17.97%What is the reducing agent in the following equation? 2 Al (s) + 3 Sn2+ (aq) <-- 2 Al3+ (aq) + 3 Sn(s)
- I beleive it should be FAD>FADH2 but that is not an option, so i am not sure which it is. Is Succinate > FADH2 the same as FAD>FADH2?We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…2. (a) The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo- globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group of the BPG molecule confer strong, negative electrostatic character to the molecule. B₁-subunit 1. 2. 3. 5. 6. B₁ (b) Mutant Hemoglobin Hb Raleigh Hb Helsinki The mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or in the vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for binding BPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for Hb Raleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substituted by Ala. Hb Rahere Hb Rancho Mirage Hb Little Rock B₂ Hb Ohio Mutation Val (31)Ala Lys(382) Met Lys(382)) Thr His(143)Asp His(3143)Gln a-NHẠ Ala(142)Asp His 2 His 143 BPG His 143 Lys 82 His 2 Rank the affinity of the mutant hemoglobins for…