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EBK ORGANIC CHEMISTRY
6th Edition
ISBN: 8220103151757
Author: LOUDON
Publisher: MAC HIGHER
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Question
Chapter 27, Problem 27.51AP
Interpretation Introduction
Interpretation:
The sequence of amino acid Q is to be stated by using the given information.
Concept introduction:
The amino acid is made of two
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Students have asked these similar questions
decapeptide has the following amino acid composition:Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, ValPartial hydrolysis yields the following tripeptides:Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly.Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. From the experimental data, deduce the primary structure of the decapeptide.(b) Suggest a scheme you will follow to synthesize the dipeptide Ala-Gly.
The amino acid histidine has ionizable groups with pKą values of 1.8, 6.0, and 9.2, as shown.
H₂N-CH
T
COOH
pH
CH₂ H
lonizable -COOH
group
=
CH
COO-
H₂N-CH
1.8
pk₁
CH2
-COO-
H
-N
CH
-HisH+
COO-
+
H₂N-CH
6.0
pk₂
CH2
-His
CH
-NH
COO-
H₂N-CH
9.2
pk3
CH2
-N
-NH₂
A biochemist makes up 80 mL of a 0.11 M solution of histidine at a pH of 5.1. She then adds 60 mL of 0.10 M HCl. What is
the pH of the resulting solution?
CH
Shown below is the amino acid tyrosine in its protonated state, with the pK₂of each ionizable proton indicated.
pK₂ = 10
HO
COOH
pk = 9
pK₂ = 2
Which best represents the predominant state of tyrosine at pH 7?
a HO.
O O
OO
a
b
U
H3N
P
H₂N COOH
b
H₂N COO
с
НО.
H₂N COO
d HO.
H₂N
COO
Chapter 27 Solutions
EBK ORGANIC CHEMISTRY
Ch. 27 - Prob. 27.1PCh. 27 - Prob. 27.2PCh. 27 - Prob. 27.3PCh. 27 - Prob. 27.4PCh. 27 - Prob. 27.5PCh. 27 - Prob. 27.6PCh. 27 - Prob. 27.8PCh. 27 - Prob. 27.9PCh. 27 - Prob. 27.10PCh. 27 - Prob. 27.11P
Ch. 27 - Prob. 27.12PCh. 27 - Prob. 27.13PCh. 27 - Prob. 27.14PCh. 27 - Prob. 27.15PCh. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Prob. 27.21PCh. 27 - Prob. 27.22PCh. 27 - Prob. 27.23PCh. 27 - Prob. 27.24PCh. 27 - Prob. 27.25PCh. 27 - Prob. 27.26PCh. 27 - Prob. 27.27PCh. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - Prob. 27.30PCh. 27 - Prob. 27.31PCh. 27 - Prob. 27.32PCh. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - Prob. 27.35PCh. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - Prob. 27.39PCh. 27 - Prob. 27.40PCh. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - Prob. 27.43APCh. 27 - Prob. 27.44APCh. 27 - Prob. 27.45APCh. 27 - Prob. 27.46APCh. 27 - Prob. 27.47APCh. 27 - Prob. 27.48APCh. 27 - Prob. 27.49APCh. 27 - Prob. 27.50APCh. 27 - Prob. 27.51APCh. 27 - Prob. 27.52APCh. 27 - Prob. 27.53APCh. 27 - Prob. 27.54APCh. 27 - Prob. 27.55APCh. 27 - Prob. 27.56APCh. 27 - Prob. 27.57APCh. 27 - Prob. 27.58APCh. 27 - Prob. 27.59APCh. 27 - Prob. 27.60APCh. 27 - Prob. 27.61APCh. 27 - Prob. 27.62APCh. 27 - Prob. 27.63APCh. 27 - Prob. 27.64APCh. 27 - Prob. 27.65APCh. 27 - Prob. 27.66APCh. 27 - Prob. 27.67APCh. 27 - Prob. 27.68APCh. 27 - Prob. 27.69APCh. 27 - Prob. 27.70APCh. 27 - Prob. 27.71APCh. 27 - Prob. 27.72APCh. 27 - Prob. 27.73APCh. 27 - Prob. 27.74APCh. 27 - Prob. 27.75APCh. 27 - Prob. 27.76APCh. 27 - Prob. 27.77APCh. 27 - Prob. 27.78APCh. 27 - Prob. 27.79APCh. 27 - Prob. 27.80APCh. 27 - Prob. 27.81APCh. 27 - Prob. 27.82APCh. 27 - Prob. 27.83AP
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- 22-35 Why is histidine considered a basic amino acid when the pKa of its side chain is 6.0?arrow_forwardA decapeptide has the following amino acid composition:Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, ValPartial hydrolysis yields the following tripeptides:Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly.Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. Fromthe experimental data, suggest a scheme you will follow to synthesize the dipeptide Ala-Glyarrow_forward8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F Cloudyarrow_forward
- The isoelectric point of the amino acid alanine is 6.0. What form will it exist in the highest concentration at pH 6.0? H H -H H 长长长 H3C C C H3C H3C + OH OH NH₂ NH2 NH3 b C a 出 H3C NH₂ a b d H H3C- C 去 + OH NH3 earrow_forwardFinally, you want to make completely certain that you purified the correct protein and not some other protein (like biochemisnotfunase). To confirm the identity of your protein, you run a Western blot. When doing a Western, one typically needs a solution of phosphate-buffered saline, which is comprised of 10 mM phosphate buffer(pH 8.0) and 0.9% (w/v) NaCl. Describe how you would make 500 mL of this solution including the grams of sodium phosphate, monobasic and sodium phosphate, dibasic that you would need. Making the phosphate buffer is a little tricky. Be sure to use the correct ratio of monobasic and dibasic sodium phosphate to get the correct pH. The Henderson- Hasselbalch equation might come in handy here. Finally, the molecular weight of sodium phosphate, monobasic (NaH2PO4) is 119.98 g/mol and the molecular weight of sodium phosphate, dibasic (Na2HPO4) is 141.96 g/mol.arrow_forwardConsider a peptide: Glu-Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly-His If the pKa values for the sidechains of Glu, His, Arg, and Lys are 4.3, 6.0, 12.5, and 9.7, respectively, determine the net charge at the following pH values. Be sure to write the charge in front (for example, +1/2, +2, and -2). pH 3: __________ pH 8: ___________ pH 11: ___________arrow_forward
- Calculate isoelectric point (PI) of the peptide GSTSRASPRM. pKa N-terminus = 9.3; pKa R = 12.5; pKa T = 13; pKa S = 13; pKa C-terminus = 4.3.arrow_forwardHis-Met-Asp-Tyr-Phe-Ser Calculate an approximate pI (isoelectric point) for this peptide.arrow_forwardUsing the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information. Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio. Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.arrow_forward
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