1. Which types of covalent bonds are important in biochemistry (only partially covered,
2. Which types of bonds can carbon, nitrogen, hydrogen, oxygen form with each other (11)
1. Compare the functions and quaternary structures of myoglobin and hemoglobin.
both are globin proteins that bind to O2 (ligands)
bound to an iron Fe2+ atom through coordination bonds to a heme group, then
bound to the protein (noncovale
1. Name two of the most important techniques that are used to determine the 3dimensional structure of proteins. (132-134, Box 4-5)
X-ray Crystallography: x-ray beam scatters light & takes x-ray picture
NMR (nuclear magnetic resonance): placing sample in
1. Which two amino acids allow the measurement of protein concentration by simple light
Trp & Tyr
What wavelength is used?
Name two assays that are based on the development of a colored product.
Lowry Assay & Bradford Assay
1. What is the purpose of cell lysis and of differential centrifugation during protein
Cell lysis remove proteins from the cell
Differential centrifugation separate proteins from cellular
Which centrifugation steps are appr
1. What is the meaning of the term "protein tertiary structure"? (123, see also 92, Fig.
structure of a single polypeptide chain determined by long range interaction of
2. Which parts of a polypeptide chain contribute to the establishment of te
1. Which functional groups of amino acids contribute to forming a peptide bond?
-carbon group & -amino group
Are peptide bonds in water thermodynamically stable? (82)
No, reaction favors combustion.
What is the reason for the persistence of peptide bond
1. What is the meaning of the term "protein secondary structure"? (117-122, see also
92, Fig. 3-23)
-helix & -conformations generated by H-bonds between amide groups &
carbonyl oxygens of backbone
2. Which parts of a polypeptide chain mainly contribute t
1. You MUST memorize the 20 common amino acids. The structures (be able to draw on
your own), the names and the one- and three-letter codes. You should also be familiar
with the physical properties of amino acids (hydrophobic, hydrophilic, polar, charged,
1. Why are the properties of water important for biochemistry? (43-46, Table 2-2)
core of compartmentalization of biochemical reactions by membranes
participates in many biochemical reactions
determine folding of biological macromole