The octanol-water partitioning constant for TCDD is 106.8, and in fact most insecticides tend to be hydrophobic. Why is this, and what consequence does it have for the fate of stable insectides in the food chain?
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The octanol-water partitioning constant for TCDD is 106.8, and in fact most insecticides tend to be
hydrophobic. Why is this, and what consequence does it have for the fate of stable insectides in the food chain?
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- Mixtures of amino acids can be analyzed by first separating the mixture into its components through ion‑exchange chromatography. Amino acids placed on a cation‑exchange resin containing sulfonate (−SO−3)(−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. Note that the ionic attraction is more important than hydrophobicity for this column media. For each pair of amino acids, identify which will be eluted first from a cation‑exchange column using a pH 7.0pH 7.0 buffer.The enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found in bacterial cell walls. The active site of lysozyme contains two amino acid residues essential for catalysis: E35 and D52. Which of the following statements about lysozyme is true? More than one may apply The graph shows the pH-activity profile of lysozyme. 100 50 4. 6. 8. 10 pH Residue E35 exhibits general base catalysis O The pKa of E35 is approximately 4.3 O The pKa of D52 is approximately 4.5 O The optimal activity of lysozyme is approximately 5.2 Residue E35 exhibits covalent catalysis The pka of E35 is approximately 6.1 The pka of D52 is approximately 3.7 Activity (% of maximal)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 =
- 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 alanineThe α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?Succinic acid is produced by Actinobacillus succinogenes with the following medium composition (g/L): glucose, 50; yeast extract, 5; NaCl, l; Na2HPO4, 0.3; NaH2PO4, 1.4; K2HPO4, 1.5; MgC12.6H20, 0.2; CaC12.2H20, 0.23. The pH is controlled and maintained at 3.63. Estimate the range of upper limit, if 0.8% of deadband is applied. With a schematic diagram, explain how to maintain the pH throughout the fermentation process.
- An analysis done on total Mn2+ of an industrial effluent is found to be 8.5 mmol L-1. The effluent will be discharged in a lake of 15 mg L-1 fulvic acid (FA) content. What is the fraction of FA expected to bind to Manganese at pH-5. Assume that Mn2+ is the only cation present in Water Lake and that its concentration is 1/10th of that of the effluent after being diluted in the lake. Binding sites of FA = 4.5 mmol g -1 and K'f (MnFA) at pH 5 = 5.0 x 10^3 Select one: A. 0.51 B.51% C. None of the suggested answers D. 0.62 E.81%In ion-exchange chromatography, amino acids are separated on the basis of electro-static interactions and hydrophobic interactions with the resin. The chemical structure of the resin pol-ymer with a negatively charged sulfonic acid group is shown to the right. An elution profile for the aminoacids using this resin is given below. Based on the elution profile above, explain the following:You need to make a protein buffer of: . • • 100 mM NaCl 25 mM Tris 8 5% w/v glycerol • 2 mM DTT Your stock solutions are: 5 M NaCl • 2 M Tris 8 • 70% w/v glycerol • DTT @ 154.25 g/mol How would you make a 1L protein buffer Solution? Show your work and describe.
- Acetocholinesterase is an enzyme possessing a single active site that metabolizesacetylcholine with a turn over number of 1.4 x 10^4s-1. How many grams of acetylcholine(molecular formula C7NO2H16+) will 2.16 x 10^-6 g acetocholinesterase metabolize in 60minutes? (The enzyme’s molecular mass is 4.2 x 10^4 g/mol).A decapeptide was isolated from a thermophilic bacteria. Treatment of this peptide with 2- mercaptoethanol gave 2 pentapeptides. Further analysis of this peptide gave the following data: Trypsin: (M,Y), (K,Y,M), (K, 2A, 2C) Chymotrypsin: (2K, 2A, 2C, Y), (M), (Y,M) What is the primary structure of the decapeptide? Thank you.What are the relative percentage (%) of species (B) and (C) at pH 7.2? (Note: treat pka's as written, i.e., no environmental/local interaction effects) A COOH I H₂N-C-H CH₂ SH Cysteine pka₁ = 2 B COO- I H₂N-C-H CH₂ SH Cysteine C COO I H₂N-C-H pka = 8.2 CH₂ S- Cysteine pka₂ = 10.3 D COO™ H₂N-C-H CH₂ S- Cysteine