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HW 2 Fall, 2009 - 1 of 4 Biological Sciences 102 Fall 2009...

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1 of 4 Biological Sciences 102 Fall, 2009 K. Hilt Homework #2 1. Amino acid analysis is done on protein “Z”. The following results are obtained: Amino Acid Number of Residues in Protein “Z” Amino Acid Number of Residues in Protein “Z” A 13 B 13 G 12 W 6 P 5 H 12 Z 24 C 4 K 8 V 24 R 12 S 12 L 23 T 14 Y 12 F 13 a) Calculate the net charge, to the nearest 0.01, of protein “Z” at pH 7. Use the pK a ’s given in homework #1. b) What is the molecular weight of protein “Z”? Use the value of 110 Daltons as an average molecular weight of an amino acid residue. c) At pH 7, would you use a cation exchanger or anion exchange resin to bind protein Z, in order to do ion exchange chromatography? d) Does protein “Z” have quaternary structure? How would you experimentally confirm this? 2. Would Sanger’s N-terminal chemistry work if the DNP-labeled N-terminal residue was extracted using diethylether with 6 N NaOH instead of diethylether with 6 N HCl? Explain. 3. Amino acid analysis of one mole of a peptide yields two moles of methionine, two moles of cysteine, one mole of arginine, and one mole of alanine. Determine the sequence of this peptide from the following information: a) treatment of the intact peptide with phenylisothiocyanate, followed by acid hydrolysis yields PTH-A; b) treatment of the peptide with cyanogen bromide yields a single amino acid (M) and a pentapeptide; c) treatment of the original peptide with trypsin yields a single product; d) treatment with mercaptoethanol also yields a single product; but e) treatment with trypsin followed by treatment with mercaptoethanol yields two products.
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