Exam1-2007 - _ Name (Last, First) BIO 361 _ SOLAR ID FALL...

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__________________________________ _____________________________________ Name (Last, First) SOLAR ID 1 BIO 361 EXAM 1 FALL 2007 VERSION 1 NAME:_________________________________________________ ID:_____________________________________________________ 1. Write Your name and ID on all pages 2. Write all answers in pen only 3. Make sure your exam has six pages including this cover page Page 2 _______________ Page 3 _______________ Page 4 _______________ Page 5 _______________ Page 6 _______________ Total _______________ Maximum of 99 points
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__________________________________ _____________________________________ Name (Last, First) SOLAR ID 2 For many of the following questions, the notation used follows certain standard “rules” – the amino acids are identified by three letter abreviations; a dash between two amino acids indicates that they are linked in a peptide bond, whereas commas separating amino acids indicate that they are present, but not necessarily linked in the order they are written (in general, amino acids separated by commas are listed in alphabetical order); the amino-terminal end is always written on the left and the carboxyl-terminal end is always written on the right. I. (3 points each) For the following peptides, indicate which statements are true (TRUE) and which are false (FALSE): A. Tyr-Arg 1._______ It is likely that this dipeptide could have been liberated from a larger polypeptide through the action of chymotrypsin. 2. _______ This dipeptide would stick to a column of sulfonated polystyrene more tightly than the dipeptide Ser-Arg. 3. _______ This dipeptide would stick to an anion exchange column of DEAE-cellulose more tightly at pH 9 than at pH 7. 4. _______ If this dipeptide were liberated by enzymatic cleavage from a so-called “integral” membrane protein, the Arg would be more likely to be exposed on the surface of the original protein than the Tyr. 5. _______ This dipeptide would not move in an electrophoretic field at pH values between 10 and 13. B. Ser-Phe 6. _______ If this dipeptide were liberated from a larger polypeptide through the action of trypsin, it must have been located at the C-terminus of the original peptide. 7. _______ Using the technique of “reverse phase” or hydrophobic interaction chromatography, this peptide would be eluted more easily than the dipeptide Ser-Gly. 8. _______ If this dipeptide were liberated from a larger polypeptide through the action of chymotrypsin, it is possible that if the larger polypeptide had first been reacted with dansyl chloride before enzymatic digestion, the dipeptide would have a dansyl group attached. 9. _______ This dipeptide would barely move in an electrophoretic field over a wide pH range
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Exam1-2007 - _ Name (Last, First) BIO 361 _ SOLAR ID FALL...

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