Campbell Biology (11th Edition)
11th Edition
ISBN: 9780134093413
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece
Publisher: PEARSON
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Textbook Question
Chapter 5.4, Problem 1CC
What parts of a polypeptide participate in the bonds that hold together secondary structure? Tertiary structure?
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What parts of a polypeptide participate in the bonds that hold together secondary and tertiary structure? Explain with the help of diagram.
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Chapter 5 Solutions
Campbell Biology (11th 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 - DRAW IT Go to Figure 5.23a and, for the top three...Ch. 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 - Which of the following categories includes all...Ch. 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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- is Tertiary protein structure come from secondary structure？How are they related？（do we need to build up a secondary structure before make it become tertiary？）arrow_forwardWhat is the approximate molecular weight of a protein with 682 amino acid residues in a single polypeptide chain?arrow_forwardDraw a polypeptide chain with the following sequence of amino acids: M-A-N-A-N-D-G-E-N-Earrow_forward
- 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 glycinearrow_forwardWhich 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_forwardConsider the structure of the tripeptide (in its fully protonated form) below. H H H + I || H₂N-C-C-N-C-C-N-C-C-OH 1 I | H CH₂ H CH₂ CH₂ T C=O OH AA1 0=0 || HC-CH3 CH3 AA2 AA3 0=C 1. Give the sequence of the tripeptide using the ONE-LETTER DESIGNATION (UPPERCASE LETTER) with NO spaces and symbols between each letter. 2. How many ionizable groups are there in the tripeptide? Give the numerical value (e.g., 10 not ten). • pH 10: {Choices: -2, -1, 0, +1, +2} 3. Which amino acid residue has one ionizable group left upon forming the tripeptide? {Choices: AA1, AA2, AA3, none, all} 4. Give the net charge of the dominant structure of the tripeptide at the given pH values. The pK, values of the amino acids are given in Table 1. • pH 4: {Choices: -2, -1, 0, +1, +2}arrow_forward
- Together, these monomers make up what type of polymer (macromolecule)? List at least three (broad) functions that these macromolecules can perform. What is an example protein that we’ve discussed that uses of these functions? Using R as the side chain, draw the basic structure of an amino acid.arrow_forwardWhat is peptide bond ?arrow_forwardDo the –H groups bound to the central carbons participate in the peptide bond?arrow_forward
- Name three kinds of bonds found in the tertiary structure of proteins?arrow_forwardAssume you have a long polypeptide chain of Gly-Val dipeptides linked end to end. Explain the likely tertiary structure of this polypeptide chain. For example, is the chain likely to form an alpha helix, a beta sheet, or some other structure? Is the structure likely to display lots of folding, or very little folding? Can you make any other predictions about the tertiary structure? Explain your reasoning in a well-developed paragraph.arrow_forwardWhich kinds of interactions can be seen in the tertiary structure of proteins?arrow_forward
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