3) Breaking of disulfide bonds may involve the following? A) Oxidation of sulfhydryl groups B) Reduction of sulfhydryl groups C) Denaturation of tertiary and/or quaternary structure D) Both B and Care correct E) All of the above 4) The following functional groups can typically participate in hydrogen bonding A) Amine B) Alcohol (hydroxyl) C) alkene groups D) All of the above are correct E) A and B only 5) During exocytosis the following typically travel to the cell membrane A) Invaginatales B) Smooth endoplasmic reticulum C) Ribosomes D) Endosomes E) None of the above 6) As a pharmaceutical researcher interested in newly isolated cannabinoid molecules, you recall that the following type of protein structure A) Is a peripheral membrane protein B) Spans the entire lipid bilayer C) Is a beta barrel motif D) All of the above are correct E) Both B and Care correct 2
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Step 1: - For each item, identify the mechanism or structural feature described and choose the most appropriate option based on standard biochemistry concepts. Show more…
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Noncovalent interactions that stabilize protein structure include A) salt bridges, B) disulfide bridges, C) electrostatic interactions with metal ions, D) the hydrophobic effect, and E) hydrogen bonding. F) All are. Characteristics of unsaturated fatty acids include A) found in plants but rarely in animals B) usually contain a double bond with trans stereochemistry C) always contain multiple double bonds D) can be converted to fats with lower melting temperature by hydrogenation E) None of these. Protein diseases can be caused by which of the following A) Activity of molecular chaperones. B) Formation of ion pairs during folding C) Mutations affecting the tertiary structure. D) All of the above are potential causes. E) None of the above are potential causes. Protein dynamics is a field of study that examines the movements with in a protein. Which experimental method would be most useful to study this type of change? A) Electrospray Ionization mass spectrometry B) X-ray absorption spectroscopy C) X-ray crystallography D) Nuclear Magnetic Resonance E) None of the above. Which of the following is accomplished by molecular chaperones? A) They bind to misfolded proteins in order to protect against heat denaturation B) They facilitate aggregation of multiple subunits of a protein during synthesis C) They ensure that hydrophobic segments do not aggregate improperly D) They expose hydrophobic segments during protein synthesis, facilitating native folding E) None of the above are accomplished by molecular chaperones. 36. ____ comprises bacterial cell walls. A) proteoglycans B) chondroitin sulfate chains C) peptidoglycans D) heparin E) pectin. 1. Which of the following statements is true? A) Fatty acids with more than 18 carbons are the most common. B) Synthesis of fatty acids occurs in 2 carbon units. C) Fatty acids with conjugated double bonds very common in plants. D) In higher plants and animals, C12 and C14 species predominate. 37. The —OH group of ____ commonly attaches O-linked oligosaccharides. A) aspartic acid B) glycine C) lysine D) threonine E) tyrosine. 38. Even though peptide groups assume the trans conformation most of the time, 10% of the time, peptide bonds involving ____ assume the cis conformation because of altered steric hindrance. A) Proline B) Glycine C) Alanine D) Tryptophan E) None of the above. 39. We use triglycerides for long-term storage of energy, rather than sugars, because triglycerides: A) Are more water soluble. B) More oxidized. C) Contain stronger covalent bonds. D) Serve also as materials for membranes. E) None of these. 40. Topology diagrams of proteins illustrate: A) The path taken by a protein through a cell B) The relative height of the protein surface C) The symmetry of subunits D) The connectivity of secondary structure elements
Madhur L.
True/False Statements: Please determine if the statements are true or false. 1. Disulfide bonding between amino acid side chains within the same protein sub-unit is considered secondary structure, while disulfide bonding between amino acid side chains of two different protein sub-units is considered quaternary structure. 2. Hydrogen bonding between two amino acid side chains within the same protein sub-unit contributes to tertiary structure, while hydrogen bonding between two amino acid side chains of two different protein sub-units contributes to quaternary structure. 3. A supersecondary structure is a compact three-dimensional protein structure of several adjacent elements of a secondary structure that is smaller than a protein domain or a subunit. Supersecondary structures can act as nucleations (or initiating points) in the process of protein folding. 4. The hydrophobic effect has the greatest influence on protein stability and is a major determinant of native protein structure; it leads to the polar side chains of amino acid residues minimizing their contact with water. Multiple Choice Questions: Please choose the most appropriate answer and fill this out on your scantron form. Only one answer is correct for each problem. 5. Protein denaturation can occur if each of the following applications are used. Please choose the best combination of matching Roman numerals (I,II,III, IV) representing terms and numbers (①②③④) representing the description. I. Heating II. pH variations III. Detergents IV. Chaotropic reagents ①Associate with nonpolar residues, interfering with hydrophobic interactions essential for native structure ② Alter ionization states of aa residue side chains, changing charge distributions, and H-bonding ③ Ions or small organic molecules like urea that increase solubility of nonpolar substances in water ④ Affects conformation. Entire polypeptide unfolds or melts (A) ①matches with I. ② matches with II. ③ matches with III. ④ matches with IV. (B) ①matches with IV. ② matches with III. ③ matches with II. ④ matches with I. (C) ①matches with II. ② matches with III. ③ matches with IV. ④ matches with I. (D) ①matches with IV. ② matches with I. ③ matches with III. ④ matches with II. (E) ①matches with III. ② matches with II. ③ matches with IV. ④ matches with I. 6. For the peptide N-Met-Gly-Pro-Glu-Arg-Asn-Ala-Ala-Pro-Ala-Gly-Pro-Gln-C. there are statements listed below. I. This peptide contains 13 amino acids in 11 peptide bonds. II. This peptide contains 13 amino acids in 12 peptide bonds. III. This peptide contains 13 amino acids in 13 peptide bonds. IV. This sequence would form an excellent α helix. V. This sequence would not form an excellent α helix. VI. At a neutral pH, the charge of this peptide is 0 VII. At a neutral pH, the charge of this peptide is -1 The true statements above include: (A) I, V, VI (B) II, IV, VI (C) II, V, VI (D) III, IV, VII (E) III, V, VII
Adi S.
Which of the following statements are correct? Explain your answers. A. The active site of an enzyme usually occupies only a small fraction of the enzyme surface. B. Catalysis by some enzymes involves the formation of a covalent bond between an amino acid side chain and a substrate molecule. C. $A \beta$ sheet can contain up to five strands, but no more. D. The specificity of an antibody molecule is contained exclusively in loops on the surface of the folded light-chain domain. E. The possible linear arrangements of amino acids are so vast that new proteins almost never evolve by alteration of old ones. F. Allosteric enzymes have two or more binding sites. G. Noncovalent bonds are too weak to influence the threedimensional structure of macromolecules. H. Affinity chromatography separates molecules according to their intrinsic charge. I. Upon centrifugation of a cell homogenate, smaller organelles experience less friction and thereby sediment faster than larger ones.
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