Which of the following is FALSE? Select one: a. The hydrogen bonding in a beta-sheet is between strands rather than within strands. b. The two main types of secondary structure are the alpha-helix and beta-sheet structures c. The hydrogen bonding in a beta-sheet is within strands rather than between strands. d. Alpha-helix is maintained by hydrogen bonds
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- Which is a difference between an alpha-helix and a beta-pleated sheet? Select one: a. An alpha-helix contains mainly amino acids with polar R-groups while a beta- pleated sheet contains mainly amino acids with non-polar R-groups. b. An alpha-helix contains disulfide bonds while a beta-pleated sheet contains ionic bonds. c. An alpha-helix has non-covalent bonds between amino acids near each other in the sequence while a beta-pleated sheet has non-covalent bonds between amino acids far apart in the sequence. d. An alpha-helix has a spiral shape while a beta-pleated sheet has a compact zig-zag shape.A protein is made up for two polypeptides that differ in shape. Each polypeptide has one domain. Which of the following is NOT true? a. the protein is stabilized by hydrogen bonds b. the two polypeptide are encoded by the same gene c. the protein has quaternary structure d. none of the above e. the protein is a heterodimerWhich of the following describes the tertiary structure of proteins? A. Helices and sheets formed from hydrogen bonds between the amino acids of polypeptides B. The functional domains that form from interactions between different parts of the polypeptide C. The association of multiple polypeptides D. The linear sequence of amino acids making up the polypeptide
- The major secondary structure seen in collagen is: a) alpha helix b) beta sheet c) collagen helix d) random coil or nonrepetitive The major secondary structure seen in hemoglobin is: a) alpha helix b) beta sheet c) collagen helix d) random coil or nonrepetitive Although all of these play a part in protein folding, the one which contributes the most is: a) salt bridges b) hydrogen bonds c) Van der Waals interactions d) hydrophobic effectWhat is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.Define the following terms: a. salt bridge b. allosteric transition c. molecular disease d. protein denaturation e. α-helix
- Denaturation of a protein A. adds hydrogen bonds to the primary level of protein structure. B. breaks hydrogen bonds in the primary level of protein structure. C. adds hydrogen bonds to the secondary and tertiary levels of protein structure. D. breaks hydrogen bonds in the secondary and tertiary levels of protein structure.Which of the following represents a NON-covalent bond? A) phosphodiester bond B) pairing of an adenine and a thymine in double stranded DNA C) binding of an hydroxyl group to the 3' carbon of ribose. D) linkage between a nitrogenous base and a ribose sugar in a nucleotideWhich of the following statements about electron microscopy are true? a) Most existing protein structures have been resolved using electron microscopy b) Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c) The smaller a protein, the easier it is to solve its structure with electron microscopy d) By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein e) The first protein structure with true atomic resolution was solved using electron microscopy last year
- Which of the following best describes a phospholipid? A. They contain a phosphate group in the place of one fatty acid B.The heads are polar C.They are energy storage molecules in the cell D. The tails are non-polarWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycineWhich of the following are involved in protein secondary structure? select one or more : a. van der waal forces b. Disulfide bridges c. Hydrogen bonds d. Peptide bonds