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