Mixtures of amino acids can be analyzed by separating the mixture into its components through ion-exchange 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: ionic attraction between the sulfonate groups on the column and positively charged functional groups on the amino acids, and hydrophobic interactions between amino acid side chains and the strongly hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine the order of elution from a cation exchanger in pH 7.0 buffer. Amino acid pair Elutes first Elutes second Asp and Arg Asp Arg Lys and Met Met Lys Ala and Glu Ala Glu Gly and Leu Leu Gly Trp and Ser Trp Ser Answer Bank
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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 (see Fig. $3-17$ a) containing sulfonate $\left(-\mathbf{S O}_{3}^{-}\right)$ 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 alanine
7. Mixtures of amino acids are analyzed by first separating the mixture into its components through ion-exchange chromatography. Amino acids placed on a cation-exchange resin containing sulfonate 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) hydrophobic interactions between amino acid side chains and the strongly hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine which will be eluted first from an ion-exchange column using a pH 7.0 buffer. a) Asp and Lys b) Arg and Met c) Glu and Val d) Gly and Leu e) Ser and Ala
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