Which of the following factors do not stabilize the 3-D structure of a folded protein? O Disulfide bonds O Van der Waals interactions O Hydrogen bonds O Electrostatic interactions O Hydrophobic bonds O Metal-ion protein interactions
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- Which of the following levels of protein architecture is least likely affected by changes in pH? O Secondary Structure Quaternary Structure O Tertiary Structure O Primary StructureWhat types of interactions are possible between the side chains of the polypeptide shown below? Select all that apply: *NH, он SH SH H H N, N, N, H H H NH2 *NH, O Disulfide bonds O Hydrogen bonds lonic bonds O Hydrophobic interactionsIn the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing?
- Which is responsible for the stabilization of parallel polypeptide chains in a beta-pleated sheet conformation? Van der Waals O covalent bonding O R-group interactions H-bondingGive the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 BWhich of the following is the primary driving force for protein folding? disulfide bridges internal hydrogen-bonds the hydrophobic effect Van der Waals forces O salt bridges
- The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bondsWhich of the following constitutes the primary structure of a protein? O the folding of a polypeptide chain the polypeptide chains stacked on top of each other O the linear sequence of amino acids in a polypeptide chain several polypeptide subunitsMercury salts (Hg+2) will denature proteins by disrupting what? One or more answers is possible. H-bonds hydrophobic regions salt bridges disulfide bonds hydration layers
- 8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3The only through space covalent interaction in 3-dimensional protein structure is . 5 ..... Hydrogen bonding Peptide bond Hydrophobic interaction Van der Waals interactions Disulfide bondBased upon your knowledge of protein folding, which of the following statements would you expect to be FALSE: O The native state is the protein conformation with the most negative Gibbs free energy value. O The hydrophobic effect causes non-polar side chains to pack into the interior of a protein away from solvent. Proteins are likely to try out every possible conformation before folding into the native state. O A protein incubated in hexane (C6H14) is likely to denature and unfold. O Detergents can interact with the side chains of valine, leucine and phenylalanine.