A) Disulfide bridges B) Hydrogen bonds C) Covalent bonds D) Ionic interactions
A) Due to their extended backbone conformation B) Due to strong covalent cross-links C) Due to high-frequency atomic vibrations D) Due to their compact helical structure
A) Static and rigid alignment B) High-frequency circular rotation C) Chaotic vibrational patterns D) Low-frequency accordion-like motion
A) Raman spectroscopy B) Electron microscopy C) Fluorescence microscopy D) X-ray crystallography
A) Four to five coiled-coil strands B) Two or three short β-strands linked by short loops C) A random coil polypeptide chain D) A single long α-helix
A) Random orientation B) Perpendicular orientation C) Parallel orientation D) Antiparallel orientation
A) Irregular cone B) Square cylinder C) Flat sheet D) Regular triangular prism
A) Asp B) Gly C) Thr D) Val
A) Perfectly circular B) Larger and perfectly symmetrical C) Less regular and indented on one side D) Completely flat
A) Ten residues B) One residue C) Two residues D) Six residues
A) An amyloid plaque B) A two-sided β-helix C) A triangular β-prism D) A parallel β-sheet
A) Potassium B) Magnesium C) Sodium D) Calcium
A) GGXGXL B) GXXGXD C) GXYGXR D) GGXGXD
A) Amyloid β B) LpxA C) Pectate lyase D) Carbonic anhydrase
A) Polar/watery and nonpolar/greasy B) Acidic and basic C) Metal and nonmetal D) Solid and gaseous
A) Unusual two-strand β-helix B) Perfectly flat β-sheet C) Left-handed triangular prism D) A simple random coil
A) Aspartic protease B) Ribonuclease inhibitor C) Immunoglobulin D) Flavodoxin
A) Four B) Eight C) Six D) Two
A) Formation is unlikely during protein folding B) It requires rare amino acids C) It is unstable in aqueous solution D) It only exists in synthetic proteins
A) Beta-prism B) Beta-propeller C) Beta-barrel D) Alpha/beta sheet
A) 21345 B) 4123 C) 3214 D) 1234
A) 12345 B) 4123 C) 54321 D) 21345
A) Open beta-sheet B) Closed beta-barrel C) Beta-prism D) Alpha/beta sandwich
A) Flavodoxin fold B) Immunoglobulin fold C) Ribonuclease inhibitor D) SH3 domain
A) Ramachandran B) Linus Pauling C) William Astbury D) Robert Corey
A) Hydrogen bond repulsion B) The size of the side chains C) The twisting of the backbone D) Tetrahedral chemical bonding at the Cα atom
A) Approximately 6 Å B) Approximately 5 Å C) Approximately 7.6 Å D) Approximately 10 Å
A) Near (-180°, 180°) B) Near (-60°, -40°) C) Near (0°, 0°) D) Near (-135°, 135°)
A) Toward the hydrogen bonds B) Toward the N-terminus C) Toward the C-terminus D) Toward the side chains
A) Parallel B) Random C) Antiparallel D) Mixed
A) A circular loop with 20 atoms B) A linear chain with 3 atoms C) An amide ring with 11 atoms D) A planar rectangle with 5 atoms
A) Alzheimer's disease B) Diabetes C) Asthma D) Hypertension
A) Beta-turns B) Beta-twists C) Beta-coils D) Beta-bulges
A) A glycine-rich turn B) A hydrophobic pocket C) A proline-rich hinge D) A helical region
A) TIM barrel B) Beta-barrel C) Greek key fold D) Beta-propeller
A) Circular twist B) Right-handed twist C) Left-handed twist D) Random coil twist
A) A letter of the Greek alphabet B) A sequence of Greek amino acids C) A historical Greek mathematician D) A pattern in Greek ornamental artwork
A) Inverse B) Left-handed C) Neutral D) Right-handed
A) Forming the hydrophobic core B) Binding to DNA C) Acting as a flexible hinge D) Catalyzing chemical reactions |