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

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
KEY _______________________________ _____________________________________ Name (Last, First) SOLAR ID 1 BIO 361 EXAM 1 FALL 2007 VERSION 1 NAME:_____________KEY ________________________________ 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
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
KEY _______________________________ _____________________________________ 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.___F____ It is likely that this dipeptide could have been liberated from a larger polypeptide through the action of chymotrypsin. 2. ___T____ This dipeptide would stick to a column of sulfonated polystyrene more tightly than the dipeptide Ser-Arg. 3. ___F____ This dipeptide would stick to an anion exchange column of DEAE-cellulose more tightly at pH 9 than at pH 7. 4. ___F____ 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. ___F____ This dipeptide would not move in an electrophoretic field at pH values between 10 and 13. B. Ser-Phe 6. ___T____ 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. ___F____ Using the technique of “reverse phase” or hydrophobic interaction chromatography, this peptide would be eluted more easily than the dipeptide Ser-Gly. 8. ___T____ 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. ___T____ This dipeptide would barely move in an electrophoretic field over a wide pH range
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 09/28/2009 for the course BIO 361 taught by Professor Lake during the Spring '08 term at SUNY Stony Brook.

Page1 / 6

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

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online