Parallel and anti-parallel beta sheets are found in proteins, but more often the latter. This is because: a. Hydrogen bonds are intermolecular in parallel, vs intramolecular for anti-parallel b. Hydrophobic interactions are the primary mode of stabilization in anti-parallel. c. The hydrogen bonding pattern is different in anti-parallel, and more directionally stabilized than parallel. d. Parallel beta sheets are only found in membrane proteins. e. None of the above 22. Which of the following is most likely to destabilize a beta sheet? A. Leu B. Asn C. Pro D. Ser E. Ala 23. lon exchange chromatography separates proteins based on a. pH b. mass c. charge d. hydrophobicity e. none of the above 24. Four proteins, 1 (MW 30,000), 2 (MW 275,000), 3 (MW 10,000) and 4 (MW 55,000) are separated by gel filtration chromatography. The order of elution from the column will be: a. 1, 2, 3, 4 b. 2, 1,4,3 c. 3,1,4,2 d. 2,4,1,3 e. 2,1,3,4 25. Four proteins, 1 (pl 5), 2 (pl 9.8), 3 (pl 7) and 4 (pl 5.7) are purified using cation exchange chromatography. What is the order of elution from the column using a salt gradient? a. 1, 4, 3, 2 b. 2,3,4,1 c. 3,1,4,2 d. 2,4,1,3 2,1,3,4

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Parallel and anti-parallel beta sheets are found in proteins, but more often the latter. This is
because:
a. Hydrogen bonds are intermolecular in parallel, vs intramolecular for anti-parallel
b. Hydrophobic interactions are the primary mode of stabilization in anti-parallel.
c. The hydrogen bonding pattern is different in anti-parallel, and more directionally
stabilized than parallel.
d. Parallel beta sheets are only found in membrane proteins.
e. None of the above
22. Which of the following is most likely to destabilize a beta sheet?
A. Leu
B. Asn
C. Pro
D. Ser
E. Ala
23. lon exchange chromatography separates proteins based on
a. pH
b. mass
c. charge
d. hydrophobicity
e. none of the above
24. Four proteins, 1 (MW 30,000), 2 (MW 275,000), 3 (MW 10,000) and 4 (MW 55,000) are
separated by gel filtration chromatography. The order of elution from the column will be:
a. 1, 2, 3, 4
b. 2, 1,4,3
c. 3,1,4,2
d. 2,4,1,3
e. 2,1,3,4
25. Four proteins, 1 (pl 5), 2 (pl 9.8), 3 (pl 7) and 4 (pl 5.7) are purified using cation exchange
chromatography. What is the order of elution from the column using a salt gradient?
a. 1, 4, 3, 2
b. 2,3,4,1
c. 3,1,4,2
d. 2,4,1,3
2,1,3,4
Transcribed Image Text:Parallel and anti-parallel beta sheets are found in proteins, but more often the latter. This is because: a. Hydrogen bonds are intermolecular in parallel, vs intramolecular for anti-parallel b. Hydrophobic interactions are the primary mode of stabilization in anti-parallel. c. The hydrogen bonding pattern is different in anti-parallel, and more directionally stabilized than parallel. d. Parallel beta sheets are only found in membrane proteins. e. None of the above 22. Which of the following is most likely to destabilize a beta sheet? A. Leu B. Asn C. Pro D. Ser E. Ala 23. lon exchange chromatography separates proteins based on a. pH b. mass c. charge d. hydrophobicity e. none of the above 24. Four proteins, 1 (MW 30,000), 2 (MW 275,000), 3 (MW 10,000) and 4 (MW 55,000) are separated by gel filtration chromatography. The order of elution from the column will be: a. 1, 2, 3, 4 b. 2, 1,4,3 c. 3,1,4,2 d. 2,4,1,3 e. 2,1,3,4 25. Four proteins, 1 (pl 5), 2 (pl 9.8), 3 (pl 7) and 4 (pl 5.7) are purified using cation exchange chromatography. What is the order of elution from the column using a salt gradient? a. 1, 4, 3, 2 b. 2,3,4,1 c. 3,1,4,2 d. 2,4,1,3 2,1,3,4
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