1. Name and draw two derivatives of amino acids beyond the 20 common amino
acids.

2. What effects the efficiency of enzymatic reaction(describe those)?

3. CJD and early-onset Alzheimer’s Disease was shown to be transmittable through the injection of HGH. What would that suggest about the brain-blood barrier?

Which of these component parts are readily soluble in the bloodstream and which are not? Monosaccharides, amino acids, glycerol, fatty acids, triacylglycerols, sterols. Explain.

Compare amino acid metabolism in plants with that in mammals, in terms of where the amino acids come from, the main kinds of things plants do for amino acid metabolism, versus the main things mammals do.

Three modifiable health behaviors that contribute to heart disease include:

Which of the following help(s) to protect against cancer?

The Healthy Hunger Free Kids Act passed in 2010 was designed to improve the nutritional quality of school lunches. This includes:

Essential amino acids _____.

1. Frequently when an enzyme or protein is heated above about 60C it loses its biological activity. Describe in molecular terms what is happening to the protein.

2. Which amino acids form disulfide bonds? What role do these bonds play in determining protein conformation?

3. What type of bonds are important in stabilizing an α helix? Explain.

4. Where are the R-groups found in an α helix? Why?

5. Glycine is found as every third amino acid in the helical regions of type I collagen. Why? Is glycine a major component of α helices?

6. Kinetically, how do allosteric enzymes differ from enzymes that display Michaelis-Menten kinetics?

7. When [S] is less than Km, v is first order with respect to [S]. What does this mean?

8. Below is the titration curve for Asp. The pKa values are 2.0 (COOH), 3.9 (side chain), 9.9 (NH ).
Identify the isoelectric point.
The point at which the pH = pKa of the amino group.
The pH ranges where buffering is best. Why?

1. What feature of amino acids give protein their structure and function?
2. Why do phospholipids spontaneously form bi-layer membranes?
3. Does RNA base pair? Explain.
4. What area of biology studies how DNA works?
5. What are the monomers of protein, nucleic acid, and starch?
6. What are the bonds between amino acids called?

Glycine and proline are both non-polar amino acids, and both are very likely to be found at the surface of proteins. What physical characteristic of each is responsible for this observation?

1) Both glycine and proline are small.
2) Glycine is small, and proline is rigid.
3) The side chains of both these amino acids make favorable interactions with molecules near the surface of proteins.
4) Both amino acids make strong interactions with each other and therefore are likely to be found next to each other in a protein.

Experiment 2: Transcription and Translation 1. Use a pen or pencil to write a five word sentence using no more than eight different letters in the space below. 2. Now, use the red, blue, green, and yellow beads to form “codons” (three beads) for each letter in your sentence. Then, create codons to represent the “start, “space” and stop” regions within your sentence. Write the sentence using the beads in the space below: 3. How many beads did you use? 4. Assign one Pop-It® bead to represent each codon. You do not need to assign a Pop-It® bead for the start, stop and space regions. These will be your amino acids. 5. Connect the Pop-It® beads to build the chain of amino acids that code for your sentence (leave out the start, stop, and space regions). 6. How many different amino acids did you use? 7. How many total amino acids did you use?

Deduce the sequence of a heptapeptide that contains the amino acids Gly, His, Tyr, Ser, Ala, Met, and Arg, from the following experimental data. Edman degradation cleaves Ala from the heptapeptide, and carboxypeptidase forms His and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms His, Ala, Tyr, and the tripeptides Ser-Gly-Met and Gly-Met-Arg.

7 amino acids total

Starting with the amino acids in the following peptide, Asn-Leu-Gly-Ile-Tyr-Val-Gln-Gly-Leu (Only really need this for question two)

1. Describe (in words) the degradation of any one of the following (Leu, Ile, Tyr, Val) to citric acid cycle and/or ketogenic products and the degradation of two of the following (Asn, Gly, Gln) to pyruvate or citric acid cycle intermediate.

2. Provide details for the incorporation of any two of the amino groups from the above amino acids into urea