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Week 2

09/20/07

QuestionsAnswers
Q: The primary structure of a protein is its _______. A: Sequence of amino acids.
Q: The secondary structure of a protein is its _______. A: Interactions between adjacent amino acids.
Q: What are the two types of secondary structures? A: Alpha-helix and beta-pleated sheets.
Q: What is the tertiary structure of a protein? A: Its 3D shape... How the protein folds upon itself.
Q: What is the quaternary structure of a protein? A: How a series of proteins fit together.
Q: Give an example of a quaternary structure. A: Hemoglobin.
Q: What type of bonds are involved in primary structures? A: Peptide bonds.
Q: What type of bonds are involved in secondary structures? A: Hydrogen bonds (between amine and carbonyl groups within the peptide backbone.
Q: What type of bonds are involved in tertiary structures? A: They could be covalent, ionic, hydrogen (between amino acid side chains), or hydrophobic.
Q: What type of bonds are involved in quaternary structures? A: They could be covalent, ionic, hydrogen (between amino acid side chains), or hydrophobic.
Q: What are the structural classification of proteins? A: Fibrous, globular, and transmembrane.
Q: Give two examples of a fibrous protein. A: Keratin and collagen.
Q: True or false? Fibrous proteins are insoluble. A: True!
Q: Give two examples of a globular protein. A: Myoglobin and hemoglobin.
Q: Where would you find transmembrane proteins? A: Embedded in the lipid bilayer of plasma membranes extending from one side of the membrane to the other side.
Q: Changes in the _______ of proteins will alter function. A: Shape.
Q: Cystic fibrosis involves a defective _______. A: Cl- channel.
Q: Familial hypercholesterolemia involves a defective _______. A: LDL receptor.
Q: What two amino acids would you NOT see in an alpha-helix? A: Proline and glycine.
Q: An alpha-helix makes a complete turn every _______ amino acids. A: 3.6
Q: In an alpha-helix the R-groups of the amino acids face to the _______. A: Outside.
Q: Is an alpha-helix a right or left handed helical shape? A: Right-handed. (I saw an old test question that mentioned D-amino acids... remember, we are talking only about L-amino acids here)
Q: What does a beta-sheet consist of? A: They consist of pairs of chains lying side by side.
Q: What stabilizes a beta-pleated sheet? A: Hydrogen bonds between the carbonyl oxygen atom on one chain and the -NH group on the adjacent chain.
Q: How are beta-pleated sheet arranged? A: In an anti-parallel fashion.
Q: What is the most common non-repetitive secondary structure? A: The beta-turn which is a reverse turn or hairpin bend. Proline and glycine are common here.
Q: A protein is said to be _______ when it loses its activity. A: Denatured.
Q: Are intracellular and extracellular domains hydrophilic or hydrophobic? A: Hyrophilic.
Q: True or false? The tertiary structure of transmembrane proteins often has two hydrophilic domains and one hydrophobic domain. A: True!
Q: The hydrophobic membrane spanning domain are typically what specific structure? A: An alpha-helix.
Q: What is a quaternary structure? A: Complexes of two or more polypeptide chains held together in precise ratios and with a precise 3D configuration.
Q: Where would you find myoglobin? A: In muscle tissue.
Q: What is the function of myoglobin? A: Oxygen storage.
Q: Myoglobin can bind to how many oxygen molecules? A: One.
Q: What is the structure of myoglobin? A: A globin chain and a single heme ring.
Q: Where would you find hemoglobin? A: In RBCs.
Q: What is the function of hemoglobin? A: Oxygen transportation.
Q: Hemoglobin can bind to how many oxygen molecules? A: Four.
Q: What is the structure of hemoglobin? A: Four globin chains (2 alpha & 2 beta) and four heme rings.
Q: What is the abbreviation for hemoglobin? A: Hb.
Q: Myoglobin is considered a _______ protein. A: Monomeric.
Q: Hemoglobin is considered a _______ protein. A: Tetrameric.
Q: In deoxyhemoglobin each heme residue contains the ferrous form of iron (Fe2+). What stabilizes the iron? A: Histidine.
Q: In O2 hemoglobin what stabilizes the oxygen? A: A distal histidine.