What is the name of the amino acid shown below?

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Presentation transcript:

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

Which of the amino acids shown below is SER ? 2

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

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

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

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

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

Glycine has no R group True False B

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

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

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

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

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

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

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)

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

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

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

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

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

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.

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

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)

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

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

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

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

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.