Escolar Documentos
Profissional Documentos
Cultura Documentos
002
2. Lysine
a. has an epsilon amino group
b. can be acetylated on its side chain
c. is abbreviated L
d. a and b
e. a and c
4. All of the statements about the classification of these amino acids are correct EXCEPT:
a. Aspartic acid and asparagine are acidic amino acids.
b. Alanine and valine are neutral, nonpolar amino acids.
c. Serine and glutamine are polar, uncharged amino acids.
d. Lysine and arginine are basic amino acids.
e. Tyrosine and phenylalanine are aromatic amino acids.
7. At physiological pH, the ratio of positively to negatively charged amino acid residues in
proteins in general is approximately
a. 3:1
b. 2:1
c. 1:1
d. 1:2
e. 1:3
8. If the side chain pka of an Asp residue is shifted to 4.5 by the microenvironment, what fraction
of the residue will exist as the conjugate base at pH 5.5?
a. 0.09
b. 0.25
c. 0.50
d. 0.82
e. 0.91
9. Which of the following properly ranks the non-covalent interactions in order of increasing
strength?
a. ionic, hydrogen bond, van der Waals
b. van der Waals, hydrogen bond, ionic
c. van der Waals, ionic, hydrogen bond
d. hydrogen bond, van der Waals, ionic
e. cannot be determined since ionic interactions and hydrogen bonds often vary in
strength
10. Assuming typical pKas for its residues, what charge is carried by the peptide FREEENERGY
at pH 8?
a. +0.5
b. +1.0
c. -2.0
d. -1.5
11. Which of the following peptides would have the largest extinction coefficient at 280 nm?
a. PAVYWC
b. WNAWMG
c. PFWPGA
d. SFAFTT
e. YMHGYH
12. The tetrameric structure of hemoglobin is an example of which level of protein structure?
a. 1st
b. 2nd
c. 3rd
d. 4th
e. 5th
13. For the reaction below at 25º C, Gº = -18 kJ/mol. What is Keq for this reaction? R is 8.31
J/Kmol
AC+D
a. 2.6 x 104
b. 2.6 x 104 M
c. 1.4 x 103
d. 1.4 x 103 M
e. 1.7 x 103 M-1
14. For the reaction below at 25º C, Gº = -52 kJ/mol and Hº = -12 kJ/ mol. What is Sº for
this reaction? R is 8.31 J/Kmol
AC+D
a. +134 J/K mol
b. -134 J/K mol
c. - 24 J/K mol
d. +37 J/K mol
e. - 37 J/K mol
15. If the conjugate [base]/[ acid] ratio for a weak acid is 1000/1, what is the pH of the solution?
a. pI + 1
b. pKa + 2
c. pKa + 3
d. pI - 2
e. pKa - 3
16. An interaction between two subunits of a protein was determined to have a ΔG°’= -57.05
kJ/mol. What is the Keq for the reaction at 25°C?
a. 1.02
b. 1.32
c. 10-10
d. 1010
e. cannot determine from given information
17. Which of the following proteins would emerge first from a CM-cellulose column run at pH
6.5?
a. A (Mr 23,500; pI 7.0)
b. B (Mr 125, 200; pI 7.5)
c. C (Mr 93,650; pI 8.3)
d. D (Mr 54,500; pI 9.1)
e. E (Mr 12,300; pI 10)
19. Based upon the following reactions, what would be the ΔG°’ for the formation of ATP from
phosphoenolpyruvate and ADP?
a. -93.7 kJ/mol
b. -30.7 kJ/mol
c. +30.7 kJ/mol
d. +93.7 kJ/mol
e. cannot determine from given information
21. Estimate the pH of the resulting solution prepared by mixing 1.0 mole of solid disodium
phosphate (Na2HPO4) and 1.25 mole of hydrochloric acid. The pKa values for phosphoric acid
are 2.1, 7.2, 12.4.
a. pH < 2.1
b. pH = 2.1
c. 2.1 < pH < 7.2
d. pH = 7.2
e. 7.2 < pH < 12.4
26. The optimal distance for a van der Waals interaction is:
a. a lot less than the sum of the van der Waals radii
b. slightly less than the sum of the van der Waals radii
c. the sum of the van der Waals radii
d. slightly more than the sum of the van der Waals radii
e. a lot more than the sum of the van der Waals radii
27. Two-dimensional gel electrophoresis separates proteins based on ________, and is typically
________.
a. size and pI, analytical
b. size and pI, preparative
c. size and hydrophobicity, analytical
d. size and hydrophobicity, preparative
e. none of the above
28. (2.5 pts) Explain how hydrophobic interactions make the entropy of a system more favorable.
1.5 pts if it was noted that the entropy of a system becomes more favorable because when
hydrophobic interactions occur LESS water molecules are organized at the surface of the
hydrophobic molecule
a. pKa
pKa = -log Ka where Ka is the acid dissociation constant
OR
pKa is the pH at which the concentration of the conjugate base is equal to the concentration of
the acid
b. pI
pI is the pH at which the amino acid or protein has a net charge of zero
[If mention isoelectric point get 1 pt; if mention average of two pKa values get 1 pt]
c. ΔG°’
The free energy change at standard state conditions and pH 7.0. This means that all reactants and
products are at a starting concentration of 1 M, except [H+] which is at 10-7M.
[If mention standard state and pH 7 without reference to 1 M concentrations get 2 pts; if mention
free energy get 0.5 pts]
d. Amphipathic
Molecule containing both polar and non-polar parts
[If suggest only applies to amino acid or protein the get 2 pts]