Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
3rd Edition
ISBN: 9780134895727
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky
Publisher: PEARSON
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Textbook Question
Chapter 3.5, Problem 2CC
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 3 Solutions
Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
Ch. 3.1 - How are gasoline and fat chemically similar?Ch. 3.1 - Which molecules in Figure 3.4a re isomers? For...Ch. 3.1 - Prob. 3CCCh. 3.1 - Prob. 4CCCh. 3.2 - How many molecules of water are needed to...Ch. 3.2 - WHAT IF? Suppose you eat a serving of fish. What...Ch. 3.3 - Write the formula for a monosaccharide that has...Ch. 3.3 - A dehydration reaction joins two glucose molecules...Ch. 3.3 - WHAT IF? After a cow is given antibiotics to treat...Ch. 3.4 - Compare the structure of a fat (triglyceride) with...
Ch. 3.4 - Why are human sex hormones considered lipids?Ch. 3.4 - Prob. 3CCCh. 3.5 - Why does a denatured protein no longer function...Ch. 3.5 - What parts of a polypeptide participate in the...Ch. 3.5 - WHAT IF? Where would you expect a polypeptide...Ch. 3.6 - DRAW IT Go to Figure 3.27a and, for the top three...Ch. 3.6 - Prob. 2CCCh. 3.7 - How would sequencing the entire genome of an...Ch. 3.7 - Given the function of DNA, why would you expect...Ch. 3 - Which functional group is not present in this...Ch. 3 - MAKE CONNECTIONS Which chemical group is most...Ch. 3 - Prob. 3TYUCh. 3 - Which of the following statements concerning...Ch. 3 - Prob. 5TYUCh. 3 - The structural level of a protein least a fleeted...Ch. 3 - Enzymes that break down DNA catalyze the...Ch. 3 - Prob. 8TYUCh. 3 - The molecular formula for glucose is C6H12O6. What...Ch. 3 - Construct a table that organizes the following...Ch. 3 - Prob. 11TYUCh. 3 - Prob. 12TYUCh. 3 - FOCUS ON ORGANIZATION Proteins, which have diverse...Ch. 3 - Prob. 14TYUCh. 3 - SYNTHESIZE YOUR KNOWLEDGE Given that the function...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Explain Tertiary Structure Is the Overall Folding of a Polypeptide Chain and Why?arrow_forwardWhat is meant by “polarity” of a polypeptide chain and by “polarity” of a chemical bond? How do the meanings differ?arrow_forwardWhat is the minimum number of polypeptide chains necessary for quaternary structure to exist?arrow_forward
- 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_forwardWhich 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_forward
- 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_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_forwardTogether, 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_forward
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