quiz 2 - STUDENTID BioBM331 QUIZ2a 9/12/07

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STUDENT ID BioBM331 QUIZ 2 a 9/12/07 1. (11 pts) Match the left column with the best right column description. Use each right column letter ONCE. ___ comparison with proteins of already known function A. has weak directional constraint ___ a protein + its prosthetic group B. membrane-bound protein ___ “breaks” an alpha helix C. special short sequence of AA ___ must be closely related to another protein D. amphipathic helix ___ highly directional interaction of Phe-Phe E. proline ___ nonpolar AA point toward protein interior F. ring stacking ___ signal to import a protein into the nucleus G. a protein crystal ___ is approximately 50% water H. zinc finger ___ can be recognized from primary structure I. holoprotein ___ Lys + sidechain binding to carbonyl group J. do this with a new AA sequence ___ nonpolar AA are on the outside K. isoenzyme (isozyme) 2. (10 pts) Draw all the atoms of the dipeptide Gly-Gly (sidechain is H), at pH 7 . pKa of terminal amino is 8, that of terminal carboxyl is 4. Draw an arrow and a label to indicate which bond(s) along the peptide backbone have partial double bond character. Draw an arrow and a label to show which bond(s) allow the φ rotation, which bond(s) allow the ψ rotation. 3. (4 pts) Answer the following questions about the Ramachandran Map that is shown to the right. Each tiny x represents a φ , ψ combination found for the protein called Protein-331. Circle the one best answer in a and in b. a. P-331 secondary structure could possibly be: i. some α -helix together with some β -sheet ii. entirely α -helix iii. entirely β -sheet b. One φ , ψ combination is found far from the others. i. this
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This note was uploaded on 09/08/2008 for the course BIOBM 3310 taught by Professor Feigenson,gw during the Fall '07 term at Cornell University (Engineering School).

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quiz 2 - STUDENTID BioBM331 QUIZ2a 9/12/07

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