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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- The lipid shown here is produced by certain microorganisms that live in extremely warm environments, such as hot springs. Assuming that this lipid makes up a portion of the organism’s membrane lipids, would the organisms produce more of this lipid or less of this lipid as the temperature increased from 45°C to 65°C?Casein, a protein in milk, has a molecular formula C38H57O9N9. Determine the total BOD, carbonaceous BOD, and nitrogenous BOD of casein in units of “grams BOD per gram of casein”The net charge on the most prevalent form of bisphosphoglycerate in blood is what?
- what are the molecular descriptors of phosphatidylinositol? LogP: Molar Refractivity: Polar Surface Area: Geometrical Diameter: Number of Hydrogen Bond Acceptors (HBA1):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 alanineMixtures 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.
- Propanamide and methyl acetate have about the same molar mass, both are quite soluble in water, and yet the boiling point of propanamide is 486 K, whereas that of methyl acetate is 330 K. Explain.Although nonpolar compounds tend to dissolve and remain in fatty tissues, polar substances are more water soluble, and more readily excreted into an environment where they may be degraded by other organisms. Explain why methoxychlor is more biodegradable than DDT.in the Isoelectric Precipitation of Proteins: Casein from Milk - A student while performing the casein precipitation using isoelectric pH, observed maximum precipitation at a pH=3.5. What could have happened during the experiment which have led to such an observation ?
- Numerous research has been conducted to determine how the sequence and structural characteristics of thermophile proteins contribute to their increased stability. Numerous research groups have conducted statistical comparisons between heat-labile and thermostable proteins.(b) What should a protein scientist do if they realized that an enzyme is sensitive to heat?It is possible to make a buffer that functions well near pH7 using citric acid, which contains only carboxylate groups. Explain.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: