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 3.5, Problem 3CC
WHAT IF? Where would you expect a polypeptide region rich in the amino acids valine, leucine, and isoleucine to be located in a folded polypeptide? Explain
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MAKE CONNECTIONS Considering the chemical characteristics of the amino acidsvaline and glutamic acid (see Figure 5.14), propose a possible explanation for the dramaticeffect on protein function that occurs when valine is substituted for glutamic acid.
WHAT IF? DRAW IT Draw a tRNA with the anticodon3¿-CGU-5¿. What two different codons could it bind to?Draw each codon on an mRNA, labeling all 5¿ and 3¿ends, the tRNA, and the amino acid it carries.
4. Let’s build a polypeptide chain
a. Using your arsenal of 4 amino acids, write out the primary structure of an 8 amino acid long polypeptide that you might be called amphipathic and thus allow it to form a micelle in aqueous solution, identify amino acid 1 through 8 as well as the location of the amino and carboxy termini of the polypeptide.
b. Explain why this polypeptide would be considered amphipathic and draw what the micelle might look like in water.
c. Taking amino acids 3, 4, and 5, draw the molecular structure of this particular stretch of polypeptide chain. Along the backbone linkage of the polypeptide identify the peptide bonds with a PB, the bonds with free rotation FR, and bonds with limited rotation LR.
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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- WHAT IF? In eukaryotic cells, mRNAs have been foundto have a circular arrangement in which proteins holdthe poly-A tail near the 5¿ cap. How might this increasetranslation efficiency?arrow_forwardYes or no? Is sequence of riboprobe identical to the mrna produced by gene in situ hybridization? does column of purification in DNA allow it to flow while other molecules are trapped ?arrow_forwardVISUALIZE Sketch a pyrimidine nucleotide subunit that would be found only in RNA. Circle and label the three components that make up this type of nucleotide. Explain what changes in the functional groups of this subunit would have to occur for it to be found in a DNA molecule.arrow_forward
- MATHEMATICAL Calculate the isoelectric point of each of the following amino acids: glutamic acid, serine, histidine, lysine, tyro- sine, and arginine.arrow_forwardLearning Objectives Identify a peptide bond, the N-terminus (amino-terminus) and C- terminus (carboxyl-terminus) of a polypeptide in a series of linked amino acids. Describe the four levels of protein structure (primary, secondary, tertiary, and quaternary), what types of bonding interactions hold each level together, and how a protein’s structure relates to its cellular function. Link the chemical structures of amino acid R groups to the types of interactions they could form in the folded structure of a protein. Hypothesize the likely consequence of environmental conditions on the folded structure. Recognize secondary structure elements when proteins are represented in different ways (e.g. ball-and-stick structures, ribbon diagrams). Define these terms: enzyme, enzyme activity, active site, substrate, enzyme substrate complex, product, denature. Explain with molecular detail how some conditions affect enzyme activity.arrow_forwardMATHEMATICAL Sketch a titration curve for the amino acid lysine, and indicate the pKa values for all titratable groups. Also indicate the pH at which the amino acid has no net charge.arrow_forward
- 5. If we have a protein that has a molar extinction coefficient of 17900 M-1cm-1 at 280nm.(a) By looking at the amino acid composition of the protein, we know it has 1 Tyr in it, but some how the professor had forgotten how many Trps where in the protein. Work out the number of Trps in the protein, given that the molar extinction coefficient at 280nm is 5500 M-1cm-1 for Trp and 1400 M-1cm-1 for Tyr. (b) If the absorbance at 280 nm of a solution of the above protein is 0.56, what is the concentration of the protein in solution, given that the pathlength of the cuvette is 1cm?arrow_forwardWHAT IF? A certain mutation in E. coli changes the lacoperator so that the active repressor cannot bind. Howwould this affect the cell’s production of β-galactosidase?arrow_forwardPls help ASAP, thank you! "An alpha-helical structure within a protein is stabilized mostly by"arrow_forward
- WHAT IF? Imagine a protein that functions in the ERbut requires modification in the Golgi apparatus beforeit can achieve that function. Describe the protein’s paththrough the cell, starting with the mRNA molecule thatspecifies the protein.arrow_forward1CFD CALCIUM-FREE CALMODULIN How long is the protein’s primary sequence?Does this protein have any secondary, tertiary and/or quaternary structures present?Are there any molecular additions to this protein that are not amino acarrow_forward1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.arrow_forward
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