Brock Biology of Microorganisms (15th Edition)
15th Edition
ISBN: 9780134261928
Author: Michael T. Madigan, Kelly S. Bender, Daniel H. Buckley, W. Matthew Sattley, David A. Stahl
Publisher: PEARSON
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Textbook Question
Chapter 6.1, Problem 2MQ
- Why are most DMA-binding proteins specific to certain chemical groups within the DMA?
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Chapter 6 Solutions
Brock Biology of Microorganisms (15th Edition)
Ch. 6.1 - What is protein domain?Ch. 6.1 - Why are most DMA-binding proteins specific to...Ch. 6.1 - Describe why a protein that binds to a specific...Ch. 6.2 - Why is negative control so named?Ch. 6.2 - How does a repressor inhibit the synthesis of a...Ch. 6.2 - Induction is considered the opposite of enzyme...Ch. 6.3 - Prob. 1MQCh. 6.3 - Prob. 2MQCh. 6.3 - What is the difference between an operon and a...Ch. 6.4 - Prob. 1MQ
Ch. 6.4 - Prob. 2MQCh. 6.4 - Explain how the lac operon is both positively and...Ch. 6.4 - Prob. 1CRCh. 6.5 - What is the major difference between...Ch. 6.5 - How do transcriptional activators in Archaea often...Ch. 6.5 - Explain how the Pyrococcus furiosus TrmBL1...Ch. 6.5 - Prob. 1CRCh. 6.6 - What are kinases and what is their role in...Ch. 6.6 - Prob. 2MQCh. 6.6 - Prob. 1CRCh. 6.7 - What are the primary response regulator and the...Ch. 6.7 - Why is adaptation during chemotaxis important?Ch. 6.7 - How does the response of the chemortaxis system to...Ch. 6.7 - Adaptation allows the mechanism controlling...Ch. 6.8 - What advantage do quorum-sensing systems confer on...Ch. 6.8 - Prob. 2MQCh. 6.8 - Prob. 3MQCh. 6.8 - How can quorum sensing be considered a regulatory...Ch. 6.9 - Which Escherichia coli genes are activated and...Ch. 6.9 - Prob. 2MQCh. 6.9 - What are some other conditions that trigger the...Ch. 6.9 - Explain the sequence of molecular events that...Ch. 6.10 - Prob. 1MQCh. 6.10 - Prob. 2MQCh. 6.10 - Prob. 3MQCh. 6.10 - Prob. 1CRCh. 6.11 - Prob. 1MQCh. 6.11 - Prob. 2MQCh. 6.11 - Prob. 3MQCh. 6.11 - What are the mechanisms by which regulation by...Ch. 6.12 - What happens when a riboswitch binds the small...Ch. 6.12 - What are the major differences between a repressor...Ch. 6.12 - What is the mechanism by which a riboswitch...Ch. 6.13 - Why does attenuation control not occur in...Ch. 6.13 - Prob. 2MQCh. 6.13 - Prob. 1CRCh. 6.14 - What is feedback inhibition?Ch. 6.14 - Prob. 2MQCh. 6.14 - Prob. 3MQCh. 6.14 - Describe how feedback inhibition is reversible.Ch. 6.15 - What types of covalent modifications commonly...Ch. 6.15 - Prob. 2MQCh. 6.15 - Explain the role of an anti-sigma factor.Ch. 6.15 - Which nucleotides are commonly used to covalently...Ch. 6 - What would happen to regulation from a promoter...Ch. 6 - Most of the regulatory systems described in this...Ch. 6 - Many amino acid biosynthetic operons under...Ch. 6 - How would you design a regulatory system to make...
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- How can I distinguish between orthosteric, allosteric and cryptic ligand binding sites?arrow_forwardTrypsin cleaves proteins on the carboxyl side of lysine. Trypsin inhibitor has a lysine residue, and binds to trypsin, yet it is not a substrate. Explain.arrow_forwardDiisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195. Which statement is true of DIPF's inhibitory mechanism? DIPF randomly modifies all serine residues on the protein, and if enough is added, the serine in the active site will eventually be modified. DIPF approaches serine 195 more closely than other substrates. DIPF looks like the substrate for chymotrypsin and binds in the active site as a competitive inhibitor. Serine 195 is in an environment that gives it a higher than normal reactivity with respect to DIPF.arrow_forward
- Consider, for example, that a particular serine residue is phosphorylated to activate the protein. In the lab, a similar effect is achieved by mutating this residue to either a D (aspartic acid) or E (glutamic acid). What could be the reason?arrow_forwardProtein structure and function: a) Name two common post-translational modifications of proteins in the cell that will affect their structure/function. b) What are prions? Briefly describe their structure and function. C) Explain the principles of protein folding and significance of urea and Bmercaptoethanol in the experimental procedures addressing this question.arrow_forwardWhat amino acid residues are phosphorylated on the intracellular domain of a VEGFR? What amino acid residues are phosphorylated on the intracellular domain of a VEGFR? Glutamic Acid Serine Tyrosine Valinearrow_forward
- Why are structural analogs of sugar molecules (such as Oseltamivir and zanamivir) effective in treatment of influenza-virus infection?arrow_forwardThe nuclear import of proteins larger than 40 kDa requires the presence of what amino acid sequence? Describe the mechanism of nuclear import. How are nuclear transport receptors able to get through the nuclear pore complex?arrow_forwardWhat is the role of a protease? Why is chymotrypsin considered to be a serine protease?arrow_forward
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