How does the coplanar nature of the peptide bond impact the overall structure of D O a. a. It facilitates the stacking of aromatic side chains. O b. It promotes the flexibility of the protein backbone. Oc. It restricts the formation of secondary structures. C. Od. It allows for the easy formation of disulfide bonds. It constrains the rotation around the peptide bond, influencing protein folding.
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- Why do some proteins contain D-amino acids? A. D-amino acids will determine the binding of the protein to its interacting partners. B. D-amino acids will determine whether the structure will be recognized and digested by naturally occurring enzymes C. D-amino acids determines the reactions the proteins will undergo. D. D-amino acids determines the solubility of the protein in aqueous solution. OE. A combination of D and L-amino acids is necessary for the proper folding of protein structures in aqueous solutions.What is the general characteristic of protein domains? A. All protein domains exhibit both a and B structures B. Protein domains constitute supersecondary structures that have specific biological functions in proteins. C. Most protein domains can be hydrolyzed from parent polypeptide chains while retaining functions and/or structures that are conserved. D. Protein domains constitute the structural block from which the protein is built E. Protein domains contain motifs that are the binding sites for prosthetic groups such as heme, or the iron-sulfur clusters.Which statements explain the primary difference between the structure of a nucleic acid and the structure of a protein? O A nucleic acid has alternating base pairs. A protein has alternating peptides O Nitrogen bases orm the backbone of a nucleic acid. Peptides form the backbone of a protein O Nucleotides link together to form a nucleic acid. Amino acids link together to form a protein O A nucleic acid is held together by the sugar-phosphate complex. A protein is held together by the carbon-carbon bonds
- What is one of the determining factors in the three-dimensional structure of a protein? A.The location of alpha sheets and beta propellersB.The presence of another proteinC.The location of hydrophobic and hydrophilic amino acidsD.The presence of nucleic acids such as DNADraw the generalized structure of an amino acid, and a peptidebond that connects them in proteinsIn a protein, a mutation occurs and results in phenylalanine being replaced by an alanine. This would. Select one: a. Always change the primary structure of the protein, never change the tertiary structure of function. O b. Always change the primary structure of a protein, sometimes affect tertiary structure and function. c Never change the primary structure, always affect secondary and tertiary structure and function. O d. Sometimes change the primary structure of a protein, always affect the tertiary structure, and sometimes affect function.
- Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactionsDescribe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)Which of the following events would have the strongest influence on the overall three-dimensional structure of a protein? Select one: a. Valines angle away from surrounding water molecules as the protein folds b. Two polypeptide strands, running in opposite directions, form hydrogen bonds with each other Oc. Another protein sticks to its outside d. The amine and carboxylic ends of the protein chain are left unreacted Oe. Three glycines are chained together Clear my choice Previous page esc ! 1 ← 2 3 W 3 E 38 $ 4 R 5 T 80 MacBook Pro A 6 Y & 7 U 8 I 9 4 1 O 0 P TO + ( W Next pa
- Using a diagram, show why a peptide bond is planar. Why are cis peptide bonds uncommon or rate in proteins?Which level(s) of protein structure rely on ionic bonds? Based on this, explain what could happen if a negatively charged amino acid was mutated to an uncharged, nonpolar, hydrophobic amino acid. A scientist is interested in determining whether a new weight loss drug adds any benefit for overweight people following a strict diet and exercise program. Would this experiment use a placebo? Explain why or why not and indicate which group would receive the placebo (if there was a placebo).How would adding acid to a non-buffered solution be most likely to affect protein structure? Select one: a. Adding acid would disrupt the primary structure of the protein b. Adding acid would cause the protein to become a lipid c. Adding acid would cause the protein to become a carbohydrate d. Adding acid would disrupt the secondary and tertiary structure of the protein