Multiple ChoiceThe primary building blocks (monomers) of proteins are: a) Glucose molecules.b) Lipids.c) Nucleotides.d) Amino acids.e) None of these.20665Has a video solution.
Multiple ChoiceWhich two functional groups are always found in amino acids?a) Carbonyl and amino groups.b) Carboxyl and amino groups.c) Amino and sulfhydryl groups.d) Hydroxyl and carboxyl groups.45097Has a video solution.
Multiple ChoiceWhat term is used for an amino acid chain that has greater than 50 covalently linked amino acids?a) Protein.b) Peptide.c) Amino acid.d) Polypeptide.18004Has a video solution.
Multiple ChoiceThe specific amino acid sequence in a protein is its:a) Primary structure.b) Secondary structure.c) Tertiary structure.d) Quaternary structure.19925Has a video solution.
Multiple ChoiceWhich of the following is true of protein structure?a) Peptide bonds are formed by hydrolysis.b) Peptide bonds join the amine group on one amino acid with the R group of another amino acid.c) Secondary protein structures are caused by hydrogen bonding between atoms of the peptide backbone.d) Tertiary protein structure emerges when there is more than one polypeptide in a protein.243371Has a video solution.
Multiple ChoiceWhat is the role of a chaperone protein?a) Assist in RNA and DNA folding.b) Assist in membrane transport.c) Assist in protein denaturation.d) Assist in dehydration synthesis reactions.e) Assist in protein folding or re-naturing.14795Has a video solution.
Multiple ChoiceThe overall three-dimensional shape of a single polypeptide is called its __________. 326
Multiple ChoiceWhich of the following lists ranks these molecules in the correct order by size from smallest to largest? 4571
Multiple ChoiceEnzyme molecules require a specific shape to perform their catalytic function. Which of the following might alter the shape of an enzymatic protein? 382
Textbook QuestionWhat two functional groups are bound to the central carbon of every free amino acid monomer? a. an R-group and a hydroxyl group b. an N—H group and a ═(C═O) group c. an amino group and a hydroxyl group d. an amino group and a carboxyl group413Has a video solution.
Textbook QuestionWhat type of bond is directly involved in the formation of an α-helix? a. peptide bonds between amino acid residues b. hydrogen bonds between amino acid residues c. van der Waals interactions between nonpolar residues d. disulfide bonds between cysteine residues270Has a video solution.
Textbook QuestionWhat type of information is used to direct different polypeptides to fold into different shapes?262Has a video solution.
Textbook QuestionThe structural level of a protein least affected by a disruption in hydrogen bonding is the a. primary level. b. secondary level. c. tertiary level. d. quaternary level.764Has a video solution.
Textbook QuestionIf a cell were to use only 10 of the 20 possible amino acids, how much effect would you expect this to have on protein diversity? Calculate and compare the number of different sequences that can be generated by randomly assembling either 10 or 20 amino acids into peptides that are five residues long.347Has a video solution.
Textbook QuestionExplain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.311Has a video solution.
Textbook QuestionDifferent proteins are composed of different sequences of . a. sugars; b. lipids; c. fats; d. amino acids; e. carbohydrates371Has a video solution.
Textbook QuestionWhy are proteins not considered to be a good candidate for the first living molecule? a. Their catalytic capability is not sufficient for most biological reactions. b. Their amino acid monomers were not likely present in the prebiotic soup. c. They cannot serve as a template for replication. d. They could not have polymerized from amino acid monomers under early Earth conditions.358Has a video solution.
Textbook QuestionPredict the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure.317Has a video solution.
Textbook QuestionProteins may function as . a. genetic material; b. cholesterol molecules; c. fat reserves; d. enzymes; e. all of the above286Has a video solution.
Textbook QuestionBased on what you know of the peptide bonds that link together amino acid residues, why would proline's side chain reduce the flexibility of the backbone?274Has a video solution.
Textbook QuestionWhich structural level of a protein would be least affected by a disruption in hydrogen bonding? a. primary structure b. secondary structure c. tertiary structure d. quaternary structure284Has a video solution.
Textbook QuestionMake a concept map (see BioSkills 12) that relates the four levels of protein structure and shows how they can contribute to the formation of hemoglobin. Your map should include the following boxed terms: Primary structure, Secondary structure, Tertiary structure, Quaternary structure, Amino acid sequence, R-groups, αα-helices, and ββ-pleated sheets.380Has a video solution.
Textbook QuestionMost proteins are soluble in the aqueous environment of a cell. Knowing that, where in the overall three-dimensional shape of a protein would you expect to find amino acids with hydrophobic R groups?339Has a video solution.
Textbook QuestionWhat are the two types of secondary structures found in polypeptides, and what maintains them? What stabilizes the tertiary structure of a polypeptide?185Has a video solution.
Textbook QuestionHow can a cell make many different kinds of proteins out of only 20 amino acids? Of the myriad possibilities, how does the cell 'know' which proteins to make?283Has a video solution.
