Campbell Biology in Focus (2nd Edition)
2nd Edition
ISBN: 9780321962751
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 3.2, Problem 2CC
WHAT IF? Suppose you eat a serving of fish. What reactions must occur for the amino acid monomers in the protein of the fish to be converted to new proteins in your body?
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Amino acids are bonded together in a linear polymer to form peptides or proteins.
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A small peptide is shown below. Define the two ends of this peptide.
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A) I is the N terminus; II is the C terminus
B) I is the C terminus; II is the N terminus
C) I is the 5' terminus; II is the 3' terminus
D) I is the 3' terminus; II is the 5' terminus
Draw an amino acid. Join it to another amino acid via dehydration synthesis to make a dipeptide. Label all parts of each amino acid and the peptide bond.
Now draw two dipeptides one on top and one below it-connect the dipeptides on top to the ones on the bottom with a line to show that they are part of two strands of one protein molecule. Connect the two dipeptides via hydrogen bonds.
Choose all that apply. This molecule is
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one of the building blocks of protein
a nucleotide triphosphate
ATP
one of the building blocks of RNA
a protein
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one of the building blocks of DNA
a nucleic acid
a carbohydrate
the energy currency of the cell
an amino acid
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Chapter 3 Solutions
Campbell Biology in Focus (2nd 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 - Prob. 1TYUCh. 3 - Which functional group is not present in this...Ch. 3 - MAKE CONNECTIONS Which chemical group is most...Ch. 3 - Prob. 4TYUCh. 3 - Which of the following statements concerning...Ch. 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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- Combine your amino acids to show the synthesis of the following di and tripeptides. Just as we saw buildin carbohydrates last week, creating larger molecules will require dehydration synthesis reactions. Two mole will be joined together, with one contributing the H and the other the OH to form a molecule of H₂0. With t models, use the OH from the carboxyl group of one amino acid and the H from the amino group of the ne form the water molecule, and join the remaining C with the N to form the peptide bond. Dipeptide and Tripeptides Ala - Glu Ala - Glu - Gly H Structure Ho O ·NH₂ How many H₂0 molecules were produced during the synthesis? Questions 1 Describe the structure of a typical amino acid why the name "amino acid" makes sense,arrow_forwardChoose from A-F. This amino acid may serve as a phosphorylation site, and turn on or off the protein. H3N-C-H H3N-C-H CH2 H2N CH 2 H-C-OH CH2 H2C CH2 CH3 CH3 Choice "A" Choice "B" Choice "C" COO H,N-C-H H,N-C-H H3N-C-H CH2 CH2 C=CH C-NH CH2 NH | CH SH C-N Choice "E" Choice "F" Choice "D"arrow_forwardWILL UPVOTE!! What is amino acid? And what’s the relation of amino acid to proteins?arrow_forward
- . Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. (a) Based on these assumptions, about how many random-coil conforma- tions will be possible for this protein? (b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forwardDraw any pentapeptide. All C-O, C-N, and C-S bonds must be written out, as well as all N-H, S-H, and O-H atoms/bonds. Your peptide must include at least one amino acid from each of the major classes of amino acids (i.e. charged, polar, etc.). Circle each peptide bond in this peptide.arrow_forward. Assume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a "random coil," with many possible conformations. (a) What must be the sign of AS for the change: native → denatured? (b) How will the contribution of AS for native → denatured affect the favorability of the process? What apparent requirement does this impose on AH if proteins are to be stable structures?arrow_forward
- Please help me with this question. More than one answer may be correct. Elastin _______. Options: A) has a repeating structure of 3 amino acids such as Gly-Pro-X B) crosslinks with numerous other elastin peptides to make an elastic fiber C) is physically attached to the smooth endoplasmic reticulum D) is physically attached to ribosomes E) is rich in hydrophobic residuesarrow_forwardin determining the structure of a fully folded protein? involving the amino acid side chains of the polypeptide. Which has the largest effect 5. hydrogen bonding ionic interactions a) b) c) d) hydrophobic interactions van der Waals interactions none of the above The misfolded, insoluble, and aggregated proteins characteristic of Alzheimer's disease and Parkinson's disease are known as: zymogens b) c) d) e) open quaternary structure proteins protein domains amyloid deposits molecular chaperones 6.arrow_forward. Separating Glycated Hb From Normal Hb (Integrates with Chapters 5and 6.) Human hemoglobin can react with sugars in the blood(usually glucose) to form covalent adducts. The a-amino groups ofN-terminal valine in the Hb b-subunits react with the C-1 (aldehyde)carbons of monosaccharides to form aldimine adducts, whichrearrange to form very stable ketoamine products. Quantitation ofthis “glycated hemoglobin” is important clinically, especially fordiabetic individuals. Suggest at least three methods by which glycatedHb (also referred to as HbA1c) could be separated from normal Hband quantitatedarrow_forward
- Protein Concept Map Add these terms to your concept map should include these concepts and details: Structure (functional groups, shape); Monomer; Linkage; Properties; Functions; Key terms from the Partial List of Key Terms from the Minds Partial List of Key Terms essential amino acid amino acid side group/R-group peptide bond polypeptide receptor neurotransmitter hormone secondary structure tertiary structure quaternary structure fair test hydrophobic hydrophilic intermolecular force of attractionarrow_forwardSC . " V Highlight each peptide bond in the molecule below. In addition, list the common names of the smaller molecules that would be released if all the peptide bonds were hydrolyzed. You can add more rows to the table if you need to. (Note: you do not need to list water.) If there are no peptide bonds in the molecule, just check the no peptide bonds box below the drawing area. ! 1 Explanation Ono peptide bonds. Q A H₂N- CH N Add Row 2 molecules released if peptide bonds hydrolyzed (list one name per row) Check W CH₂ S X 1 option command # 3 H E D $ 4 C R F % 5 -NH–CH–COO CH₂ CH₂ V T 80 G O : ; { [ I command option + + 11 Q 11 ? 1 I E d } 1arrow_forwardAPPLICATIONS ON PROTEINS S TY Question #1: A shampoo bottle lists "partially hydrolyzed protein" as one of its ingredients. What is the difference between partially hydrolyzed protein and completely hydrolyzed protein? partially hydrolyzed protein completely hydrolyzed proteinarrow_forward
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