Bio 21 Cell Biology
List of Terms and Study Guide
For MiniExam 1, 12 February 2001
ER (endoplasmic reticulum)
common elements of living organisms
carboxyl group (carboxylic acid)
R group (side chain)
condensation reaction (dehydration synthesis)
molecular chaperone/heat shock protein
thermally induced motion
association vs dissociation
PANELS TO FOCUS ON
2-1, 2-2, 2-5, 2-7
FIGURES TO FOCUS ON
1-12, 1-14, 1-17
2-2, 2-6, 2-13, 2-20, 2-22, 2-26, 2-28
1. Know how eukaryotes differ from prokaryotes (e.g. presence of membrane-bound organelles). Know the arguments supporting the endosymbiotic origin of eukaryotic cells.
2. Be able to recognize the various components that make up a eukaryotic cell. Have a general understanding of the function of each (e.g. mitochondria generate ATP through food oxidation; plastids such as chloroplasts generate ATP through photosynthesis).
3. Be able to draw a generic amino acid and label the subgroups (R group, amino group, carboxyl group). Be able to draw an a.a. in both its ionized and unionized forms.
4. Be able to recognize the various classes of amino acids: basic, acidic (in both ionized and unionized form), nonpolar, and uncharged polar.
5. Be able to recognize interactions between amino acids that form H bonds, ionic bonds, or result in hydrophobic interactions.
6. Know the types of interactions (chemical bonds) that stabilize primary, secondary, tertiary, and quaternary levels of protein structure.
7. Be able to show how a peptide bond is formed through a dehydration synthesis (condensation reaction).
8. Be able to show how serine, threonine, and tyrosine can be targets of phosphorylation.
9. Understand the difference between a base and an acid, how they function in water,how such interactions affect the behavior of individual amino acids, and how multiple such interactions contribute to the stucture and behavior of a polypeptide or protein.
10. Know the polar (or nonpolar) nature of covalent bonds between the most common elements in living organisms (i.e., C-H, N-H, O-H).
11. Know which amino acids are capable of forming disulfide bonds (i.e., cysteine), under what conditions they will form (i.e., oxidative rather than reducing environment), and what levels of protein structure they can help stabilize (tertiary and quaternary).
12. Know the sequence of atoms and the nature of their bonds that make up the polypeptide backbone.
13. Know how to recognize the amino or N-terminus vs the carboxy or C-terminus of a polypeptide.
14. Know how to identify an alpha helix and ß pleated sheet (sometimes
referred to as simply a ß sheet). Know how these structures are stabilized
by H-bonds. Know the difference between a parallel and antiparallel ß
sheet. Know how the amino acid side chains (the R groups) are arranged in
space in both an alpha helix and ß sheet. Understand how the class
of amino acids (i.e., nonpolar, polar, or charged) forming an alpha helix
or ß sheet can make the structure hydrophilic, hydrophobic, or amphipathic.