Old Test - in class review on 2-13-09

Old Test - in class review on 2-13-09 - Old Test Reviewed...

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Old Test Reviewed on 2/13/09 Friday 1. Which a.a. does not exist in stereoisomeric form? Glutamine, glutamate, glycine , glutamic acid, cysteine 2. Which tripeptide is most likely found on surface of protein? (the one with most hydrophilic groups) Glu-lys-asp Not phe-phe-phe 3. What a.a. would make best buffer at physiological pH? Bicarbonate, phosphate, methionine, histidine , buffadine Histine only a.a. with pka close to physiological pH. Best buffer would otherwise be phosphate with pKa 6.9 4. Which is closest to net charge of the following at pH 7? Gly-glu-lys-asp-gly +_x__-__+__ -__x__- Net charge = -1 5. Phenylisothiocyanate is used to sequence protein because it: (Edman’s reagent, sequences 1 a.a. at a time, good for 20-25 a.a. before exhaustion) Readily forms cyclic hydantion Easily derivatized on solid structure 6. For asparagine and glutamine, the R side group is an amide 7. What is the pI of gly-gly-phe 9__x__x__x__2.5 pI = 9+2.5/2 = 5.75 8. Which hexapeptide yields most fragments when reacted with cyanogen bromide:
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This note was uploaded on 04/14/2010 for the course BHC 3023 taught by Professor Harmen during the Spring '10 term at University of South Florida - Tampa.

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Old Test - in class review on 2-13-09 - Old Test Reviewed...

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