CAREY: ORGANIC CHEMISTRY
10th Edition
ISBN: 9781260364002
Author: VALUE EDITION
Publisher: MCG CUSTOM
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Chapter 26.7, Problem 14P
Interpretation Introduction
Interpretation:
Assuming that each chirality center is L, the structural formula for each of the given dipeptides is to be shown in a manner that reveals the stereochemistry at the
Concept Introduction:
A peptide bond is an amide bond. A dipeptide contains two amino acids linked by a peptide bond.
It is formed between amino group of one amino acid the carboxyl group of the other amino acid.
The peptide structures are written, such that the amino group is at the left side and the carboxyl group is at the right side.
The left end of the peptide is called the N terminus and the right end is called the C terminus.
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Part 1. Aqueous 0.010M AgNO 3 is slowly added to a 50-ml solution containing both carbonate [co32-] = 0.105 M
and sulfate [soy] = 0.164 M anions. Given the ksp of Ag2CO3 and Ag₂ soy below. Answer the ff:
Ag₂ CO3 = 2 Ag+ caq) + co} (aq)
ksp = 8.10 × 10-12
Ag₂SO4 = 2Ag+(aq) + soy² (aq) ksp = 1.20 × 10-5
a) which salt will precipitate first?
(b)
What % of the first anion precipitated will remain in the solution.
by the time the second anion starts to precipitate?
(c) What is the effect of low pH (more acidic) condition on the separate of the carbonate and
sulfate anions via silver precipitation? What is the effect of high pH (more basic)? Provide appropriate
explanation per answer
Part 4. Butanoic acid (ka= 1.52× 10-5) has a partition coefficient of 3.0 (favors benzene) when distributed bet.
water and benzene. What is the formal concentration of butanoic acid in each phase when
0.10M aqueous butanoic acid is extracted w❘ 25 mL of benzene
100 mL of
a) at pit 5.00
b) at pH 9.00
Calculate activation energy (Ea) from the following kinetic data: Temp (oC) Time (s) 23.0 180. 32.1 131 40.0 101 51.8 86.0 Group of answer choices 0.0269 kJ/mole 2610 kJ/mole 27.6 kJ/mole 0.215 kJ/mole 20.8 kJ/mole
Chapter 26 Solutions
CAREY: ORGANIC CHEMISTRY
Ch. 26.1 - Prob. 1PCh. 26.2 - Prob. 2PCh. 26.2 - Prob. 3PCh. 26.3 - Prob. 4PCh. 26.3 - Prob. 5PCh. 26.4 - Prob. 6PCh. 26.4 - Prob. 7PCh. 26.4 - Prob. 8PCh. 26.5 - Prob. 9PCh. 26.6 - Prob. 10P
Ch. 26.6 - Prob. 11PCh. 26.6 - Prob. 12PCh. 26.7 - Prob. 13PCh. 26.7 - Prob. 14PCh. 26.7 - Prob. 15PCh. 26.7 - Prob. 16PCh. 26.7 - Prob. 17PCh. 26.9 - Prob. 18PCh. 26.10 - Digestion of the tetrapeptide of Problem 26.18...Ch. 26.12 - Prob. 20PCh. 26.12 - Prob. 21PCh. 26.15 - Prob. 22PCh. 26.15 - Prob. 23PCh. 26.16 - Prob. 24PCh. 26.17 - Prob. 25PCh. 26.18 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39PCh. 26 - Prob. 40PCh. 26 - If you synthesized the tripeptide Leu-Phe-Ser from...Ch. 26 - Prob. 42PCh. 26 - Prob. 43PCh. 26 - Prob. 44PCh. 26 - Prob. 45DSPCh. 26 - Prob. 46DSPCh. 26 - Prob. 47DSPCh. 26 - Prob. 48DSPCh. 26 - Prob. 49DSPCh. 26 - Prob. 50DSP
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