Campbell Biology in Focus
3rd Edition
ISBN: 9780134710679
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Rebecca Orr
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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Using Fig. as a guide, draw the complete structure of a nucleoside triphosphate before and after it becomes incorporated into a polynucleotide chain. Draw the structure that would result if the newly formed phosphodiester bond were hydrolyzed.
Consider the following peptide to answer the questions below:
A M A K K E S H I F T A I D E
What is the total charge of this peptide at pH = 5?
What is the N terminal amino acid (full name)? C terminal amino acid?
How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)?
Would this peptide be a candidate to form an alpha helix? Why or why not
What following statement is TRUE concerning motifs and domains?
a) Both motifs and domains are independently stable.
b) Domains undergo dynamic individual changes that affect the entire protein
c) B-a-ß loops, B barrels, and helix-turn-helix structure are types of domains
d) Motifs and domains are part of secondary structural elements
e) Ab initio computations predict motif folds accurately a majority of the time
My guess is B.
Chapter 3 Solutions
Campbell Biology in Focus
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
- (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α -helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40- residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?arrow_forwardConsider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins. (a) What level is shown by doublestranded DNA? (b) What level is shown by tRNA? (c) What level is shown by mRNA?arrow_forwardConsider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary)as defined for proteins.(a) What level is shown by double-stranded DNA?(b) What level is shown by tRNA?(c) What level is shown by mRNA?arrow_forward
- What is a helix-turn-helix motif? secondary structure in which an α helix is separated from a β sheet by a loop supersecondary structure in which an α helix is separated from another α helix by a turn supersecondary structure in which a β sheet is separated from a helix by a turn secondary structure in which two right-handed α helices are intertwined secondary structure in which two left-handed α helices are intertwinedarrow_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(a) How many activation cycles are needed for a protein with 150 amino acids? (b) How many initiation cycles are needed for a protein with 150 amino acids? (c) How many elongation cycles are needed for a protein with 150 amino acids? (d) How many termination cycles are needed for a protein with 150 amino acids?arrow_forward
- Consider a globular protein that contains an alpha-helix within it: a) Suppose there is a ligand binding pocket in this alpha-helix that contains residues of Leu (2), Phe (5), Gly (6), Ala (18), Tyr (22), Tyr (28), Gly (30), Cys (45), His (48) and Asp (49). What does this tell us about the likely nature or characteristics of a potential binding ligand? I said tha because 6/10 of the amino acids in this binding pocket are non-polar, that the ligand is also non-polar, but I think the question needs more description about the ligand. b) Briefly describe the driving forces and energetics behind folding of globular proteins (use terms like ΔH, ΔS, and ΔG) I said that H = -, S = +, G = - Folding driving force would likely be entropy change from non-polar residues interacting with a solvent (ex: water). Hence, non-polar residues would be buried in the globular protein structure from folding, causing entropy to increase for any liberated solvent molecules. Not 100% sure if this is correct,…arrow_forwardWhere would you expect a polypeptide region Ridge and the amino acid valine, leucine, and isoleucine to be located in a folded polypeptide? explainarrow_forwardThe following are sequences from three different alpha helices found inhuman proteins: hBak(72-87): GQVGRQLAIIGDDINR hCB1(196-210): VTASFTASVGSLFLT hCB2(248-262): LVLAVLLICWFPVL Classify each of these three helices as either a) mostly hydrophobic, b)mostly hydrophilic, or c) amphipathic. Use the helical wheel to explainyour answers. Given the character of these helices, in which part of the protein wouldyou expect them to reside?arrow_forward
- Consider a short peptide that forms an alpha-helix within a larger protein structure. Suppose that one glutamate residue at some specific position in the helix were mutated to a leucine residue. The mutation could either make the helix more stable, or less stable. i) Describe two situations in which a Glu-to-Leu mutation could make the helix more stable. ii) Describe two situations in which the Glu-to-Leu mutation could make the helix less stable. Explain briefly the basis for the stabilizing and destabilizing effect in all cases.arrow_forwardSYNZIPS are a-helices that can be used in synthetic biology to create coiled-coil interactions between two different proteins. SYNZIP1 is around 47 amino acids in length. If each turn in an a-helix is 3.6 residues in length and each turn is 5.4 Å in length, how long is SYNZIP1? Keep in mind that 1 Å = 10 nm. Present your answer in nm.arrow_forwardTwo peptide segments are shown below. Predict which one would have the most negative AG when going from an unfolded to a folded structure. Justify your choice. (i) Gly-Ala-Asn-lle-Val-Trp-Leu-Glu-Met-Phe-Val-Pro OR (ii) Ala-Gly-Lys-lle-Arg-Tyr-Thr-Cys-Val-Glu-Met-Serarrow_forward
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