Multiple ChoiceThe primary building blocks (monomers) of proteins are:2956views11rankHas a video solution.
Multiple ChoiceWhich two functional groups are always found in amino acids?6972views19rankHas a video solution.
Multiple ChoiceWhat term is used for an amino acid chain that has greater than 50 covalently linked amino acids?2643views17rankHas a video solution.
Multiple ChoiceThe specific amino acid sequence in a protein is its:2864views12rankHas a video solution.
Multiple ChoiceWhich of the following is true of protein structure?3484views17rankHas a video solution.
Multiple ChoiceThe overall three-dimensional shape of a single polypeptide is called its __________. 720views
Multiple ChoiceWhich of the following lists ranks these molecules in the correct order by size from smallest to largest? 889views1rank
Multiple ChoiceWhich of the following represents a specific description of a polypeptide? 832views1rank
Multiple ChoiceEnzyme molecules require a specific shape to perform their catalytic function. Which of the following might alter the shape of an enzymatic protein? 780views1rank
Multiple ChoiceThe α helix and β pleated sheet represent which level of protein structure? 683views2rank
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 residues601viewsHas a video solution.
Textbook QuestionWhat type of information is used to direct different polypeptides to fold into different shapes?522viewsHas 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.1361viewsHas 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.721viewsHas a video solution.
Textbook QuestionExplain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.637viewsHas a video solution.
Textbook QuestionDifferent proteins are composed of different sequences of . a. sugars; b. lipids; c. fats; d. amino acids; e. carbohydrates735viewsHas 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.920viewsHas a video solution.
Textbook QuestionPredict the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure.654viewsHas a video solution.
Textbook QuestionProteins may function as . a. genetic material; b. cholesterol molecules; c. fat reserves; d. enzymes; e. all of the above620viewsHas 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?638viewsHas 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 structure789viewsHas 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.767viewsHas 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?808viewsHas 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?569viewsHas 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?690viewsHas a video solution.
Textbook QuestionMark the following statements as true or false. If a statement is false, correct it to make a true statement.d. Proteins are composed of strings of fatty acids linked by glycosidic bonds.135viewsHas a video solution.
Textbook QuestionAn enzyme is a:a. biological catalyst that increases the concentration of the products.b. biological catalyst that increases the concentration of the reactants.c. chemical that is used in a reaction, after which it can no longer be used by the cell.d. biological catalyst that works by bringing its substrates closer to their transition states.146viewsHas a video solution.
Textbook QuestionWhy is it important for a protein to maintain its structure? What is it called when a protein loses its structure?209viewsHas a video solution.