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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Chapter 14.1, Problem 1CC
MAKE CONNECTIONS In a research article about alkaptonuria published in 1902, Garrod suggested that humans inherit two “characters” (alleles) for a particular enzyme and that both parents must contribute a faulty version for the offspring to have the disorder. Today, would this disorder be called dominant or recessive? (See Concept 11.4.)
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nzymes play a fundamental role in cell function.
Regarding the biochemistry of enzymes, which of the following statements is correct?
A.
Most enzymes can bind and react with a wide range of different substrate molecules.
B.
Enzymes increase the rate of a spontaneous reaction by lowering the ΔG.
C.
Enzymes increase the enthalpy (H) of the products compared to the reactants.
D.
Enzymes increase the number of molecules that get to the transition state.
1. Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red.
A. Suppose research has shown that amino acid 82 in the red shaded region is lysine, an amino acid with a positively-charged side chain. This lysine is critical for catalysis. Other studies have found that amino acids 12 and 62 in the blue region are both phenylalanine, an amino acid with a nonpolar side chain, and are critical for substrate binding. These amino acids are relatively close in the active site but are separated by 20-70 amino acids in the primary structure. Using what you know about protein structure, explain how amino acids separated in the primary structure can come close together in the active site.
B. Use this information and figure 4.2 in your book to answer the following questions: Do you think changing amino acid 82, lysine, an amino acid with a positively-charged side…
. The allosterically regulated enzyme ATCase binds aspartic acid as a
substrate and acylates the a-amino group. Succinate acts as a competitive
inhibitor of ATCase because it binds the active site but can't be acylated. The
dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the
accompanying figure. Panel (b) shows the effect of increasing [succinate]
on v, when [Asp] is held at a low concentration (see thick vertical arrow in
panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see
thin horizontal arrow). Explain the shape of the curve in panel (b). Why
does v, increase initially, before decreasing at higher [succinate]?
Co0-
COO
CH2
CH,
HC -NH,
CH,
COO
COO
Asp
Succinate
[Asp)
[Succinate]
[Asp] in
experiment b
(a)
(b)
Chapter 14 Solutions
Campbell Biology in Focus (2nd Edition)
Ch. 14.1 - MAKE CONNECTIONS In a research article about...Ch. 14.1 - What polypeptide product would you expect from a...Ch. 14.1 - DRAW IT The template strand of a gene contains the...Ch. 14.2 - What is a promoter? Is it located at the upstream...Ch. 14.2 - What enables RNA polymerase to start transcribing...Ch. 14.2 - WHAT IF? Suppose X-rays caused a sequence change...Ch. 14.3 - Given that there are about 20,000 human genes, how...Ch. 14.3 - How is RNA splicing similar to how you would watch...Ch. 14.3 - WHAT IF? What would be the effect of treating...Ch. 14.4 - What two processes ensure that the correct amino...
Ch. 14.4 - Discuss the ways in which rRNA structure likely...Ch. 14.4 - Describe how a polypeptide to be secreted is...Ch. 14.4 - WHAT IF? DRAW IT Draw a tRNA with the anticodon...Ch. 14.5 - What happens when one nucleotide pair is lost from...Ch. 14.5 - Prob. 2CCCh. 14.5 - WHAT IF? DRAW IT The template strand of a gene...Ch. 14 - In eukaryotic cells, transcription cannot begin...Ch. 14 - Prob. 2TYUCh. 14 - The anticodon of a particular tRNA molecule is A....Ch. 14 - Prob. 4TYUCh. 14 - Which component is not directly involved in...Ch. 14 - Prob. 6TYUCh. 14 - Prob. 7TYUCh. 14 - Prob. 8TYUCh. 14 - Fill in the following table: Type of RNA Functions...Ch. 14 - SCIENTIFIC INQUIRY Knowing that the genetic code...Ch. 14 - Prob. 11TYUCh. 14 - FOCUS ON INFORMATION Evolution accounts for the...Ch. 14 - SYNTHESIZE YOUR KNOWLEDGE Some mutations result in...
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- C)|Myth: The specificity of an enzyme for its substrate is explained by the lock and key hypothesis. Fact: The lock and key hypothesis is outdated! What is our current model for understanding regarding how enzymes recognize and bind to substrates?arrow_forwardNew anti-cancer agents are being developed that target fatty acid synthase (FASN) due to a requirement for lipid synthesis to promote tumor cell replication. Describe why an enzyme inhibitor targeted to the following sites would or would not work to inhibit lipid synthesis. Explain your answer. If you’re not sure whether it will work, make an argument for and against it working. ACP site on FASN The dimer interface between monomers of FASN Targeting FASN to mitochondrial matrixarrow_forwardWhich statements are true? Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.arrow_forward
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