Campbell Biology (10th Edition)
10th Edition
ISBN: 9780321775658
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 4TYU
The 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.
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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.
Protein 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 c
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
Chapter 5 Solutions
Campbell Biology (10th Edition)
Ch. 5.1 - What are the four main classes of large biological...Ch. 5.1 - How many molecules of water are needed to...Ch. 5.1 - WHAT IF? If you eat a piece of fish, what...Ch. 5.2 - Write the formula for a monosaccharide that has...Ch. 5.2 - Prob. 2CCCh. 5.2 - WHAT IF? After a cow is given antibiotics to...Ch. 5.3 - Compare the structure of a fat (triglyceride) with...Ch. 5.3 - Why are human sex hormones considered lipids?Ch. 5.3 - Prob. 3CCCh. 5.4 - What parts of a polypeptide participate in the...
Ch. 5.4 - Prob. 2CCCh. 5.4 - WHAT IF? Where would you expect a polypeptide...Ch. 5.5 - Prob. 1CCCh. 5.5 - DRAW IT In a DNA double helix, a region along one...Ch. 5.6 - How would sequencing the entire genome of an...Ch. 5.6 - Given the function of DNA, why would you expect...Ch. 5 - What is the fundamental basis for the differences...Ch. 5 - Compare the composition, structure, and function...Ch. 5 - Why are lipids not considered to be polymers or...Ch. 5 - Explain the basis for the great diversity of...Ch. 5 - What role does complementary base pairing play in...Ch. 5 - Prob. 5.6CRCh. 5 - Prob. 1TYUCh. 5 - The enzyme amylase can break glycosidic linkages...Ch. 5 - Prob. 3TYUCh. 5 - The structural level of a protein least affected...Ch. 5 - Enzymes that break down DNA catalyze the...Ch. 5 - The molecular formula for glucose is C6H12O6. What...Ch. 5 - Which of the following pairs of base sequences...Ch. 5 - Construct a table that organizes the following...Ch. 5 - Prob. 9TYUCh. 5 - EVOLUTION CONNECTION Comparisons of amino acid...Ch. 5 - SCIENTIFIC INQUIRY Suppose you are a research...Ch. 5 - WRITE ABOUT A THEME: ORGANIZATION Proteins, which...Ch. 5 - SYNTHESIZE YOUR KNOWLEDGE Given that the function...
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- 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 glycinearrow_forwardIn Protein structure: a). Write the name of the four levels of protein structure, b). Explain the structural characteristics at each level,arrow_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 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_forward(a) Are all proteins polymers? What is the basie unit of protein? Explain the formation of Zwitterion in a-amino acid. (b) Count the number of peptide bonds in the below structure. -R-N-C-R-N-C-R-N-C-R-N-C- wwww H H H Harrow_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_forward
- Which of the following statements is true about the quaternary structure of a protein? A) The quaternary structure of a protein is based on how polypeptide subunits interact with one another. B) The quaternary structure of a protein is affected by hydrogen bonds. C) The quaternary structure is the overall shape of a protein. D) The quaternary structure is driven by a- helices and B-pleated sheets. E) The quaternary structure is found in all proteins.arrow_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_forwardupvote guaranteedarrow_forward
- How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bondsarrow_forwardd) Describe what is meant by the primary structure of a protein? e) At the secondary level of structure, protein molecules will fold in either of two ways. • What are these two secondary forms of folding called? • What do these two forms look like structurally? • How is their structural arrangement stabilised? f) Describe the tertiary structure of a protein. g) Describe the biological function of the peptide hormone insulin. h) Haemoglobin is an example of a quaternary protein. Briefly describe the structure of this protein and state its biological function. Part 2 Monosaccharides and disaccharides are two of the sub-classes of Carbohydrates. Structure B shown below is a specific example of a monosaccharide. H HO Structure B CH₂OH H OH H OH H OH a) Name Structure B and describe its function within cells. b) State the name of a disaccharide that contains this molecule (Structure B) and describe its structure. c) A branched polysaccharide made up of many monomers of Structure B bonded…arrow_forwardAmino acid structure and composition: Assuming physiological pH conditions, draw the peptide backbone of a protein composed of four amino acids. The protein is a) overall positively charged b) capable of forming disulfide bond with another protein c) has two amino acid that can participate in hydrogen bond formation d) one peptide bond in cis conformation you must show the complete name, single letter abbreviation and structure of each amino acid. Make sure to highlight the peptide bond that is in cis conformationarrow_forward
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