Mindtap Biology, 1 Term (6 Months) Printed Access Card For Solomon/martin/martin/berg's Biology, 11th
11th Edition
ISBN: 9781337393096
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
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Chapter 3, Problem 9TYU
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
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Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycine
Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycine
The structural level of a protein least affected by a disruption inhydrogen bonding is the(A) primary level.(B) secondary level.(C) tertiary level.(D) quaternary level.
Chapter 3 Solutions
Mindtap Biology, 1 Term (6 Months) Printed Access Card For Solomon/martin/martin/berg's Biology, 11th
Ch. 3.1 - Describe the properties of carbon that make it the...Ch. 3.1 - Define the term isomer and distinguish among the...Ch. 3.1 - Identify the major functional groups present in...Ch. 3.1 - Explain the relationship between polymers and...Ch. 3.1 - What are some of the ways that the features of...Ch. 3.1 - Prob. 2CCh. 3.1 - Prob. 3CCh. 3.1 - Prob. 4CCh. 3.1 - Prob. 5CCh. 3.2 - Distinguish among monosaccharides, disaccharides,...
Ch. 3.2 - VISUALIZE Draw simple sketches comparing the...Ch. 3.3 - Distinguish among fats, phospholipids, and...Ch. 3.3 - Prob. 1CCh. 3.3 - Explain why the structure of phospholipids enables...Ch. 3.4 - Give an overall description of the structure and...Ch. 3.4 - Prob. 8LOCh. 3.4 - Distinguish among the four levels of organization...Ch. 3.4 - Prob. 1CCh. 3.4 - Prob. 2CCh. 3.5 - Describe the components of a nucleotide. Name some...Ch. 3.5 - VISUALIZE Sketch a pyrimidine nucleotide subunit...Ch. 3.6 - Compare the functions and chemical compositions of...Ch. 3.6 - How can you distinguish a pentose sugar from a...Ch. 3 - Prob. 1TYUCh. 3 - VISUALIZE The structures depicted are (a)...Ch. 3 - Prob. 3TYUCh. 3 - The synthetic process by which monomers are...Ch. 3 - A monosaccharide designated as an aldehyde sugar...Ch. 3 - Structural polysaccharides typically (a) have...Ch. 3 - Saturated fatty acids are so named because they...Ch. 3 - Fatty acids in phospholipids and triacylglycerols...Ch. 3 - Which of the following levels of protein structure...Ch. 3 - Which of the following associations between R...Ch. 3 - Each phosphodiester linkage in DNA or RNA includes...Ch. 3 - PREDICT Do any of the amino acid side groups shown...Ch. 3 - PREDICT Like oxygen, sulfur forms two covalent...Ch. 3 - Hydrogen bonds and van der Waals interactions are...Ch. 3 - EVOLUTION LINK In what ways are all species alike...Ch. 3 - EVOLUTION LINK The total number of possible amino...Ch. 3 - EVOLUTION LINK Each amino acid could potentially...
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- Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.arrow_forwardupvote guaranteedarrow_forwardWhat level of protein structure is determined by the following:(a) Peptide bonds between amino acids?(b) Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?(c) R group interactions that may involve Van der Waalsforces, ionic interactions, or hydrogen bonds?arrow_forward
- Which level(s) of protein structure result(s) from non-covalent interactions involving both backbone groups and side chains? (Select all that apply!) a) Primary b) Secondary c) Tertiary d) Quaternaryarrow_forwardMatch the following statements about protein structure with the proper levels of organization. (i) Primary structure (ii) Secondary structure (iii) Tertiary structure (iv) Quaternary structure (a) The three-dimensional arrangement of all atoms (b) The order of amino acid residues in the polypeptide chain (c) The interaction between subunits in proteins that consist of more than one polypeptide chain (d) The hydrogen-bonded arrangement of the polypeptide backbone.arrow_forwardProtein secondary structure is stabilized by ... a) H-bonds between functional groups on amino acid side chains. b) interactions between hydrophobic amino acid R-groups. c) H-bonds between the N-H and C=O groups of the peptide backbone. d) a and c e) a, b and carrow_forward
- In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.arrow_forwardIn Protein structure: a). Write the name of the four levels of protein structure, b). Explain the structural characteristics at each level,arrow_forwardProteins are found to have two different types of secondary structures viz. a-helix and B-pleated sheet structures. a-helix structure of a protein is stabilised by: (i) Hydrogen bonds (ii) van der Waals forces (iii) Peptide bonds (iv) Dipole-dipole interactionsarrow_forward
- Which one of the following types of bond is principally responsible for holding the α-helix shape of a protein secondary structure : A) peptide B) disulfide C) hydrogen D)ionicarrow_forwardWhich of the following features correctly describe aspects of protein structure? a) A protein possessing disulfide bonds will be more stable than a protein with the identical primary sequence lacking disulfide bonds. O b) B-sheets can only be formed from the anti-parallel arrangement of B-strands. c) Folding of a protein (tertiary structure) will typically result in a majority of the non-polar amino acids being distributed on the protein surface. d) both a and carrow_forwardProtein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be rightarrow_forward
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