ProblemSet2 - C) proteins attracting primarily salt anions...

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1. The chemical structures of four amino acids are depicted above and they are labeled I, II, III, and IV. Use your knowledge of amino acid nomenclature, structure, and chemistry to answer the following questions. Answer with the Roman numeral unless otherwise instructed. 5 points each (40 points total) A) What is the single letter code of amino acid I? B) Which of these does not carry a neutral charge at pH 7? C) Which amino acid is classified as aromatic? D) What is the three letter code of amino acid III? A) What is the isoelectric point (pI) of I? B) Which amino acid contains the indole side group? C) Which cannot form hydrogen bonds through its side group? D) Which has a polar uncharged side group? 2. The salting in of proteins can be explained by: A) salt counter-ions reduce electrostatic attraction between protein molecules B) proteins attracting primarily salt cations
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Unformatted text preview: C) proteins attracting primarily salt anions D) realing hydrophobic proteins from nonpolar tissue environments E) hydration of salt ions reducing solubility of proteins 3. A mixture of lysine and aspartic acid is applied to an anion exchange column at pH 7.5. Which amino acid will bind the column? Explain why. 4. Trypsin degradation of a peptide yields the fragments H, MNK, IMR and LMP. Cyanogen bromide treatment yields RH, RM, NKIM and LM. Deduce the sequence of the peptide. 5. It takes a minimum of about 40 amino acid residues for a polypeptide to fold into a stable structure. Explain what a stable structure means. Why does it take ~40 resides to form a stable structure? 6. The different polypeptide chains in a protein are known as------- (fill in the blank). Why do some proteins contain multiple polypeptide chains?...
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This note was uploaded on 01/31/2010 for the course CHEM chem 114A taught by Professor Gourisankarghosh during the Fall '06 term at UCSD.

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