Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 14TYK
The α helix of proteins is
- a. part of a protein’s tertiary structure and is stabilized by disulfide bridges.
- b. a double helix.
- c. stabilized by hydrogen bonds and is commonly found in fibrous proteins.
- d. found in some regions of globular proteins and is stabilized by hydrophobic interactions.
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Students have asked these similar questions
The level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide is referred to as the
A. quaternary structure.
B. secondary structure.
C. primary structure.
D. tertiary structure.
A. A macromolecule composed of one or more
polypeptides
B. The monomer of polypeptides.
C. The specific sequence of amino acids in a
polypeptide.
D. Structure of coils and/or folds of a
polypeptide strueture.
E. Structure of polypeptide resulting from
interactions between R-groups. Contributes to
unique 3D shape of molecule.
F. Two or more polypeptides interacting to form
a single functional unit.
1. Protein
2. amino acid
3. primary structure
4. secondary structure
5. tertiary structure
6. quaternary structure
Which of the following statements are correct about protein structure (select all that apply)?
A.
Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein
B.
Only amino acids with a net charge may interact with other amino acids
C.
The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role.
D.
Hydrophobic interactions play a key role in protein folding
E.
Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acids
Chapter 5 Solutions
Study Guide for Campbell Biology
Ch. 5 - Monomers are linked into polymers by ________...Ch. 5 - You can recognize a monosaccharide by its multiple...Ch. 5 - Number the carbons in the following glucose and...Ch. 5 - Prob. 4IQCh. 5 - Fill in this concept map to help you organize your...Ch. 5 - a. Draw the amino acids alanine (R group: CH3) and...Ch. 5 - In the following diagram of a portion of a...Ch. 5 - Now that you have gained experience with concept...Ch. 5 - a. Label the three parts of this nucleotide....Ch. 5 - Take the time to create a concept map that...
Ch. 5 - Prob. 1SYKCh. 5 - Prob. 2SYKCh. 5 - glycogen A. carbohydrate B. lipid C. protein D....Ch. 5 - cholesterol A. carbohydrate B. lipid C. protein D....Ch. 5 - RNA A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - collagen A. carbohydrate B. lipid C. protein D....Ch. 5 - hemoglobin A. carbohydrate B. lipid C. protein D....Ch. 5 - A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - Prob. 7TYKMCh. 5 - enzyme A. carbohydrate B. lipid C. protein D....Ch. 5 - cellulose A. carbohydrate B. lipid C. protein D....Ch. 5 - Chitin A. carbohydrate B. lipid C. protein D....Ch. 5 - Polymerization (the formation of polymers) is a...Ch. 5 - Which of the following statements is not true of a...Ch. 5 - Prob. 3TYKCh. 5 - Prob. 4TYKCh. 5 - Prob. 5TYKCh. 5 - Prob. 6TYKCh. 5 - A fatty acid that has the formula C16H32O2 is a....Ch. 5 - Prob. 8TYKCh. 5 - Prob. 9TYKCh. 5 - Prob. 10TYKCh. 5 - Which of the following molecules provides the most...Ch. 5 - Prob. 12TYKCh. 5 - What happens when a protein denatures? a. Its...Ch. 5 - The helix of proteins is a. part of a proteins...Ch. 5 - What is the best description of the following...Ch. 5 - Prob. 16TYKCh. 5 - Prob. 17TYKCh. 5 - Which of the following is true of the subunits of...Ch. 5 - Prob. 19TYKCh. 5 - If the nucleotide sequence of one strand of a DNA...Ch. 5 - How are nucleotide monomers connected to form a...Ch. 5 - Prob. 22TYK
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- Match the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsarrow_forwardA prosthetic group of a protein is a non-protein structure that is: a. a ligand of the protein. b. a part of the secondary structure of the protein. c. a substrate of the protein. d. permanently (tightly) associated with the protein. e. transiently bound to the protein.arrow_forwardProteins are the dominant structural and functional molecules in a cell. Which one of the following statements about proteins is NOT correct? A. The native conformation of a protein is usually arrived at very quickly after synthesis. B. Hydrogen bonding is the only type of bonding that gives rise to secondary structure. C. Urea denatures proteins by disrupting the interactions among non-polar (hydrophobic) amino acids D. Most proteins consist of a single polypeptide and thus do not have quaternary structure.arrow_forward
- Proteins often have regions that show specific, coherent patterns of folding or function. These regions are called: a. domains. b.oligomers. c. peptides. d. sites. e. subunits.arrow_forwardIn the α helix the hydrogen bonds: a. are roughly parallel to the axis of the helix. b. are roughly perpendicular to the axis of the helix. c. occur mainly between electronegative atoms of the R groups. d. occur only between some of the amino acids of the helix. e. occur only near the amino and carboxyl termini of the helix.arrow_forwardThe tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forward
- Which of the following statements is/are TRUE for globular proteins? A. sensitive to changes in pH & heat B. regular amino acid sequence C. soluble in water D. structural rolearrow_forwardWhich of the following is FALSE? Select one: a. The hydrogen bonding in a beta-sheet is between strands rather than within strands. b. The two main types of secondary structure are the alpha-helix and beta-sheet structures c. The hydrogen bonding in a beta-sheet is within strands rather than between strands. d. Alpha-helix is maintained by hydrogen bonds.arrow_forwardWhich 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 interactionsarrow_forward
- Which of the following is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptidearrow_forwardWhich of the following is NOT an example of protein secondary structure? a. alpha-helix b. beta sheets c. beta turn d. coiled coil e. loopsarrow_forwardWhich of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.arrow_forward
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