1. Identify each macromolecule. Circle the functional group that is characteristic of each
2. Explain what occurs when the activation energy is reduced. Hint: Characteristics of enzymes
3. a. Explain where free energy of a molecule originates from. b. ∆G = ∆H-∆T(∆S) define each term of this equation and explain what happens in a reaction if: • ∆H of a system is greater than the product of ∆T(∆S)
4. Name each base and the nucleotide formed using each base. Identify the group that distinguishes the purines from the pyrimidines.
5. Draw a ribose sugar and glucose sugar ring structure form.
6. To which group or groups of amino acids does the molecule below belong? Choose the one best answer.
a. Hydrophilic acidic b. Hydrophilic neutral c. Hydrophilic basic d. Hydrophobic neutral e. a and b f. b and c g. c and d h. d and a
7. Indicate with arrows the two atoms that would be involved in peptide bonds if the amino acid were incorporated into a protein. Be precise so that the atoms you intend are unambiguously identified.
8. This amino acid would most likely be found
a. on the outside of a folded globular protein (protein in water/fluid) forming hydrogen bonds with water or other proteins
b. on the interior of a folded globular protein excluding water from the interior of the folded protein.
9. Indicate with arrows the two atoms that would be involved in hydrogen bonds to form alpha helices if the amino acid were incorporated into a protein. Be precise so that the atoms you intend are unambiguously identified.
10. Indicate with arrows the two atoms that would be involved in hydrogen bonds to form beta sheets if the amino acid were incorporated into a protein. Be precise so that the atoms you intend are unambiguously identified.
11. Circle the group of atoms that would be involved in hydrogen bonds to form interactions between two alpha helices and one beta sheet in a single polypeptide.
12. Circle the group of atoms that would be involved in hydrogen bonds to form interactions between an alpha helices on one polypeptide and a beta sheet on a different polypeptide.
13. The molecules shown on the right are a. a base b. an acid c. a sugar d. a nucleotide e. a nucleoside f. d and e
14. Which pair or pairs of the below amino acids might be expected to be involved in replacement that does affect the tertiary structure of a protein?
a. Asp and Glu b. Leu and Val c. Arg and Lys d. Ser and Thr e. All the pairs f. None of the pairs g. More than one of the pairs but not all the pairs
15. Which amino acid is involved in cross linking proteins by disulfide bond formation?
a. When cross-linking occurs, do the sulfur groups contain hydrogens or not? b. Are the sulfur groups oxidized or reduced?
16. Based on importance to the structure of proteins and function, which bonds are most important for forming molecules from atoms living things?
a. Vander Waals forces b. Hydrogen Bonds c. Electrostatic interactions d. Covalent e. Ionic
17. Label each polypeptide with all the potential functions it can have in the cell based on the interaction in the diagram (ligand: receptor; substrate: enzyme; antigen: antibody; motor, channel).
18. Describe the difference between a protein Domain and a protein subunit.
19. Identify a protein domains or subunits in the figures below.
20. Briefly characterize Tay-Sachs Disease (gene, protein and its function, pathology of the disease). b. Describe the effect the above process would have if it occurred on the gene (from one parent) associated with your disease pathology while leaving the gene from the other parent unaffected.
21. A protein functioning as an enzyme reaches Vmax at 2 seconds per mole of substrate and has a Km of 10-9moles/liter of the substrate. A second enzyme reaches Vmax at 3 seconds but has a Km of 10-12.
Which enzyme is more specific and why?
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