exam1 - 6(1 At what pH would this peptide have a net charge...

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
12/25/09 5:48 PM http://www4.ncsu.edu/~knopp/BCH451/e09b1.htm Page 1 of 1 BCH 451 Summer 2009 Exam #1 NAME 1. Draw the predominate structures of the following molecules at the pH indicated. Be sure to include all carbon and hydrogen atoms! (7) Isoleucyl-methionyl-histidyl-arginyl-tryptophanyl-glutaminyl-cysteine @ pH = 8.9 2. (0.2 each) Circle and label all functional groups or linkages in the above peptide except for the peptide bond: 3. (0.1 each) Write the pKa by each functional group. If there is none, write “no pKa” by that functional group: 4. (0.4 each) Indicate the exact site of cleavage for chymotrypsin [using the letter “C” and an arrow] and trypsin [using the letter “T” and an arrow] in the above peptide: 5. (0.5) Calculate the pI of this peptide. [Show your setup for full credit.]:
Background image of page 1
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: 6. (1) At what pH would this peptide have a net charge of +1.66? [Show your setup for full credit.]: 7. (4) Describe the indirect effect of carbon dioxide upon the oxygen binding of hemoglobin: 8. (1.5) Describe the Lowry assay: [What is it used for and how does it work.] 9. (2) PUZZLER Dr. Knopp stated that fetal hemoglobin’s advantage is through an altered binding of 2,3 BPG. Design an experiment which would test this hypothesis: 10. (2) If a linear series of amino acids had a common values for psi of +140 degrees and for phi of -130 degrees, what can you say about the conformation and why? 11. (1 each) List and describe the properties of hydrogen bonds: 12. (1 each) Definitions: a. Left handed α-helix b. Assay c. Chromatography d. Domain e. Isomer f. Side chain g. P 50...
View Full Document

{[ snackBarMessage ]}

Ask a homework question - tutors are online