1. What is the name of the amino acid shown below?
Asp
Arg
Lys
Met
Leu C 1

2. Which of the amino acids shown below is SER ?2

3. Which amino acid is this?
Phe
His
Tyr
Trp C 3

4. Which of the following amino acids has a side chain that can form covalent cross-links in proteins?
Ser
Met
Trp
Cys
Thr D 4

5. Which of the following pairs of amino acids might form a salt bridge?
Thr, Glu
Tyr, Ser
Glu, Asp
Lys, Arg
Lys, Asp E 5

6. Which of the following amino acid side chains is polar and uncharged?
Glu
Trp
Tyr
Phe
Ile C 6

7. Which of the following groups of amino acid side chains is MOST LIKELY to be positioned into the active site of an enzyme that binds glucose as a substrate?
Gln, Asn, Ser
Val, Leu, Ile
Trp, Phe, Ile
Val, Glu, Lys
Cys, Met, Pro A
This one was the tricky
Glucose

8. Glycine has no R group
True
False B

9. Which of the following statements regarding amino acids is/are false?
Thr and Cys may be phosphorylated.
The side chain of the amino acid histidine usually acts as a base at pH 7.0.
Arg contains four nitrogens.
A and B
All of the above statements are false. A

10. Which of the following statements regarding amino acids is/are false?
Ala, Val, Leu and Ile play an important role in establishing and maintaining the 3-D structures of proteins.
Every amino acid has at least two pKa values.
When the pH of a solution is below the pKa value of an ionizable group, the unprotonated form of that group predominates.
Statements A and B are false.
All of the above statements are false. C

11. Which of the following does NOT contain a carboxamide functional group?
The amino acid Asn.
The amino acid Asp.
The dipeptide Gln-His.
All of these contain a carboxamide group.
None of these contain a carboxamide group. B

12. How many chiral carbons does Thr contain?1 2 3 C

13. Which of the following net charge best represents aspartate at pH 12?-2 -1 +1 +2 A

14. There are several amino acid side chains that are always charged at physiological pH. These are:
Gln, Asn, Lys, and Arg.
Glu, Asp, Lys, and Arg.
Lys, His, and Arg.
Glu, Asp, Lys, Arg, and His. B

15. Which of the following amino acids could form a hydrogen-bonding interaction between their sidechains?
Q and A
Q and V
Q and F
Q and I
Q and W E
C ( if you add NH—aromatic interactions)

16. How many charged functional groups are present on the peptide below at physiological pH ?1 2 3 4 5
Arg-Asp-Cys-Tyr-Gln-Val-Glu
E – 3 side chains (arg, asp, glu) and 2 terminii

17. What is the net charge of the peptide below at physiological pH?-2 -1 +1 +2
Ala-Arg-Asn-Asp-Glu-Ser-Gly B 17

18. The energy consumed in the urea cycle can be recovered from metabolism associated with this cycle.
True
False
Can’t be determined A

19. Which of the following are ways to produce glutamate?
Reductive amination of -KG
Transamination of -KG
Glutamate synthase
A and B
All of the above
A = glutamate dehydrogenase

20. The carbon skeleton of amino acids may not be used to:
Generate acetyl-CoA.
Generate glucose.
Generate urea.
Generate ketone bodies. C

21. Which of the following enzymes require ATP?
Carbamoyl phosphate synthetase I
Methionine synthase.
Arginosuccinate synthetase.
A and C.
All require ATP. D
AMC: SynthETase gives it away.

22. Which of the following amino acids are derived from pyruvate?
Leucine
Isoleucine
Lysine
Valine
i and ii
i, ii and iii
i, ii and iv
i, iii and iv
iii only C

23. Which of the following is an essential amino acids in humans?
Alanine
Asparagine
Aspartate
Arginine
D- even though we synthesize it (we use a lot more that we have capacity to make)

24. Which of the following is not an end product of amino acid catabolism?
-Ketoglutarate
Succinyl-CoA
Fumarate
Malate
Oxaloacetate D

25. Amino acids are precursors for which of the following molecules?
Porphyrins
Epinephrine
Histamine
Nitric oxide
All of the above E

26. Which of the following is the first step in amino acid degradation?
Removal of the -carboxylate group.
Removal of the -amino group.
Degradation of the carbon skeleton to a citric acid cycle intermediate. B

27. Which of the following molecules can be supplied in excess to treat a deficiency in ornithine transcarbamoylase?
Argininosuccinate
Benzoate
Phenylacetate
B and C
All of the above D

28. The combined effect of glutamine synthetase and glutamate synthase is to incorporate fixed nitrogen into an organic compound and to produce an amino acid.
True
False A.
The organic compound is -KG and the amino acid is glutamate.