Exam 1
BCMB 311, Advanced Cell Biology, Fall 2012
EXAM 1
__________________________________Name
True-False Questions (Write T or F next to the question, 1 point each)
1. A globular protein in the cytoplasm will normally be folded up in such a way that most of its non-polar sidechains are buried in the interior of the protein and most of its polar and charged side-chains are exposed on its surface. T
2. Alpha helices are stabilized by hydrogen bonds between amino acid side chains, whereas beta sheets are stabilized by hydrogen bonds between main chain amino and carbonyl groups. F
3. Protein domains are contiguous stretches of polypeptides that are capable of folding and functioning independently of the rest of the protein. T
4. In an alpha helix, approximately ¼ of the amino acids are engaged in intrachain hydrogen bonding. F
5. Alpha helices are stabilized by hydrogen bonding whereas beta sheets are stabilized by hydrophobic interactions.
F
6. In a beta sheet the side chains of adjacent amino acids face in opposite directions. T
7. In an alpha helix, the side chains of the amino acids are buried on the inside whereas the main-chain atoms are exposed to the surrounding medium. F
8. Two proteins that share the same 3-d folding pattern are always identical or very similar at the level of primary structure. F
9. The wavelength of light that causes excitation of a fluorophore is always longer than the wavelength of light emitted by the same fluorophore. F
10. In a light microscope, it is not possible to detect light from a source that is smaller than the resolution limit imposed by the wavelength of visible light. F
11. In light microscopy, it is not possible to distinguish two objects that are separated by less than about 0.2μm. T
12.The information about how a protein should fold up is contained in the primary amino sequence of the protein itself. T
13. Van der Waals interactions are too weak to contribute significantly to bonding of
EXAM 1
__________________________________Name
True-False Questions (Write T or F next to the question, 1 point each)
1. A globular protein in the cytoplasm will normally be folded up in such a way that most of its non-polar sidechains are buried in the interior of the protein and most of its polar and charged side-chains are exposed on its surface. T
2. Alpha helices are stabilized by hydrogen bonds between amino acid side chains, whereas beta sheets are stabilized by hydrogen bonds between main chain amino and carbonyl groups. F
3. Protein domains are contiguous stretches of polypeptides that are capable of folding and functioning independently of the rest of the protein. T
4. In an alpha helix, approximately ¼ of the amino acids are engaged in intrachain hydrogen bonding. F
5. Alpha helices are stabilized by hydrogen bonding whereas beta sheets are stabilized by hydrophobic interactions.
F
6. In a beta sheet the side chains of adjacent amino acids face in opposite directions. T
7. In an alpha helix, the side chains of the amino acids are buried on the inside whereas the main-chain atoms are exposed to the surrounding medium. F
8. Two proteins that share the same 3-d folding pattern are always identical or very similar at the level of primary structure. F
9. The wavelength of light that causes excitation of a fluorophore is always longer than the wavelength of light emitted by the same fluorophore. F
10. In a light microscope, it is not possible to detect light from a source that is smaller than the resolution limit imposed by the wavelength of visible light. F
11. In light microscopy, it is not possible to distinguish two objects that are separated by less than about 0.2μm. T
12.The information about how a protein should fold up is contained in the primary amino sequence of the protein itself. T
13. Van der Waals interactions are too weak to contribute significantly to bonding of