Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 26, Problem 39P
Staphylococcus nuclease is an enzyme that catalyzes the hydrolysis of DNA.
The reaction is catalyzed by Ca2+, Glu 43, and Arg 87. Propose a mechanism for this reaction. Recall that the
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Question 30 of 72
Using proper convention, provide the amino acid sequence for the following
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CH,
Ala Arg Asn Asp
Cys Glu
Gin Gly His lle Leu Lys
Met Phe Pro Ser
Thr Trp
The standard free energy change (ΔG°') for hydrolysis of fructose-l,6-bisphosphate (FBP) to fructose-6-phosphate (F-6-P) and Pi is -16.7 kJ/mol:
FBP + H2O → Fructose-6-P + Pi
The standard free energy change (ΔG°') for ATP hydrolysis is -30.5 kJ/mol:
ATP + H2O → ADP + Pi
a
What is the standard free energy change for the phosphofructokinase reaction:
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ΔG°' = -13.8 kJ/mol
b
What is the equilibrium constant for this reaction at 25.0 °C?
K'eq =
NAD+ stands for the coenzyme a. niacin adenine dinucleotide b. nicotinic acid diphosphate c. nicotinamide diphosphate d. nicotine adenosine dinucleotide e. nicotinamide adenine dinucleotide.
Chapter 26 Solutions
Organic Chemistry (8th Edition)
Ch. 26.1 - In acidic solutions, nucleosides are hydrolyzed to...Ch. 26.1 - Draw the structure for each of the following: a....Ch. 26.3 - Indicate whether each functional group of the five...Ch. 26.3 - Prob. 4PCh. 26.3 - If one of the strands of DNA has the following...Ch. 26.4 - The 2',3-cyclic phosphodiester that is formed...Ch. 26.5 - Using a dark line for the original parental DNA...Ch. 26.7 - Why do both thymine and uracil specify the...Ch. 26.9 - If methionine is always the first amino acid...Ch. 26.9 - Four Cs occur in a row in the segment of mRNA...
Ch. 26.9 - UAA is a stop codon. Why does the UAA sequence in...Ch. 26.9 - Prob. 12PCh. 26.9 - Write the sequences of bases in the sense strand...Ch. 26.9 - List the possible codons on mRNA that speciy each...Ch. 26.10 - Adenine can be deaminated to hypoxanthine, and...Ch. 26.10 - Explain why thymine cannot be deaminated.Ch. 26.12 - Which of the following base sequences is most...Ch. 26 - What nonapeptide is coded for by the following...Ch. 26 - What is the sequence of bases in the template...Ch. 26 - Prob. 20PCh. 26 - A segment of DNA has 18 base pairs. It has 7...Ch. 26 - Name the following:Ch. 26 - Prob. 23PCh. 26 - Propose a mechanism for the following reaction:Ch. 26 - The first amino acid incorporated into a...Ch. 26 - Match the codon with the anticodon:Ch. 26 - a. Using the single-letter abbreviations for the...Ch. 26 - Which of the following pairs of dinucleotides are...Ch. 26 - Human immunodeficiency virus (HIV) is the...Ch. 26 - If a mRNA contained only U and G in random...Ch. 26 - Why is the codon a triplet rather than a doublet...Ch. 26 - RNAase, the enzyme that catalyzes the hydrolysis...Ch. 26 - The amino acid sequences of peptide fragments...Ch. 26 - Which cytosine in the following sense strand of...Ch. 26 - Prob. 36PCh. 26 - Sodium nitrite, a common food preservative (page...Ch. 26 - Why does DNA not unravel completely before...Ch. 26 - Staphylococcus nuclease is an enzyme that...
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- 22-20 Show how alanine, in solution at its isoelectric point, acts as a buffer (write equations to show why the pH does not change much if we add an acid or a base).arrow_forward22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a substitution for leucine in the primary structure of a protein that would probably not change the character of the protein very much.arrow_forward22-92 Write the expected products of the acid hydrolysis of the following tetrapeptide:arrow_forward
- 22-104 Why is collagen not a very good source of dietary protein?arrow_forwardAll amino acids share a common structure, a central (alpha) carbon with four groups attached. Which of these is NOT one of the four groups attached to the alpha- carbon? O an R group an ammonium group (-NH3+) O a carboxylate group (-COO) a hydronium grouparrow_forwardShown below is a structure in which two amino acids are connected by a peptide bond. What are the names of the two amino acids in this structure? [Select TWO options.] HO NH3 Glutamine O Tryptophan O Leucine O Threonine Aspartate (a.k.a. aspartic acid) Alanine O Serine O Valine O Cysteine O Methionine O Phenylalanine O Arginine O Histidine O Tyrosine O Glutamate (a.k.a. glutamic acid) O Glycine O Proline Asparagine O Lysine OIsoleucine NH2 NH2arrow_forward
- 13. In the physiological pH range, the nitrogen in the imidazole ring can be easily protonated/deprotonated. This allows the histidine side chain to— act as a strong reducing agent. bind either H+ or OH-. function as either a general acid catalyst or a general base catalyst. interact with the guanidino group. either gain or lose an electron.arrow_forward47. A pentapeptide on complete hydrolysis yields 3 moles of glycine (R=H), 1 mole of alanine (R=CH3) and 1 mole of serine (R=CH2OH). On partial hydrolysis, the fragments are ala-gly, gly-ala and gly-ser. The pentapeptide is negative to the Sanger reaction. Draw a possible structure for the pentapeptide.arrow_forwardA protein structure is solely determined by the sequence of amino acids in the primary structure. Suppose that you were to genetically engineer a new protein by keeping the exact same sequence, but it was completely reversed in the order of amino acids compared to the original. Would the new protein have the same tertiary structure as the original? Why?arrow_forward
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