EBK BIOCHEMISTRY
6th Edition
ISBN: 9781337431200
Author: GRISHAM
Publisher: CENGAGE LEARNING - CONSIGNMENT
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Question
Chapter 24, Problem 21P
Interpretation Introduction
Interpretation:
A series of three consecutive reactions in the synthesis of linoleic acid from palmitic acid that embody chemistry like three reactions in the tricarboxylic acid cycle needs to be identified.
Concept Introduction:
Palmitic acid has 16 carbon and linoleic acid is a 18 carbon fatty acid and linoleic contains two C=C double bonds. One cycle of fatty acid synthesis is required to undergo to convert palmitic acid to linoleic acid.
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The titration curve of alanine shows the ionization of two functional groups with pK values of 2.34 and 9.69, corresponding to
the ionization of the carboxyl and the protonated amino groups, respectively. The titration of di-, tri-, and larger oligopeptides of
alanine also shows the ionization of only two functional groups, although the experimental pK values are different. The table
summarizes the trend in pK values.
Amino acid or peptide
Ala
Ala-Ala
pKj
pk₂
2.34
9.69
3.12
8.30
Ala-Ala-Ala
3.39
8.03
Ala-(Ala)-Ala, n ≥ 4
3.42
7.94
Modify the molecules to show the oligopeptide Ala-Ala-Ala. You can modify the molecules by moving, adding,
deleting, or changing atoms, bonds, or charges.
C
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Templates
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H с N 0
S
Cl
H
H
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H CH3
H
CH,
H CH₂
Complete the statements about the the pK, values of the Ala-Ala-Ala oligopeptide.
The pK₁ value of 3.39 is associated with the
-COO group of Ala-Ala-Ala.
The pK2 value of 8.03 is associated with the -NH
group of Ala-Ala-Ala.
Erase
Q2 Q…
Facts from the bacterium
mals and to dept kan apa
in a peptide with antidic properties. This peptide
complex with
the call membrance of other hacterial species, leading in bacterial death
The structure of the peptide has been determined from
(a) Cmplete acid hydes of the peptide, followed by amino acid analys, yielded quiar anunt of Lan, Om, Pfx, Prxa,
and Wall Cmtiti, an amino acid od prosentin pockets but present in some peptides. Com has the tracture
H
*H,N-CH-CH-CH, -C- COO
(b) The weight of the peptide in approximately 1,200 Th
(c) The peptide failed to undergo hydrolysis when treated with the
Hydrolysis of the carbonyl-terminal residue of a polypeptide une
"NH,
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year. This call
there Pro or the police does not contain a froz
(d) Treatment of the peptide with 1-haw-2,4-dicherer (11N1), followed by complete hydrolysis and
ched only from and the derivative
NO,
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CH, CH, C
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(Hint: The 2,4-diphenyl derivative involves the amino group of a side chain rather than the…
Electrophoresis
Macmillan Learning
Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a
single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and
lane 2 contains chymotrypsin pre-treated with performic acid.
1
2
Why does performic acid treatment of chymotrypsin generate three bands in lane 2?
°
Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues.
The three peptides are impurities in the original chymotrypsin sample.
Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues.
Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin.
Correct Answer
Chapter 24 Solutions
EBK BIOCHEMISTRY
Ch. 24 - Explaining the Stoichiometry of Fatty Acid...Ch. 24 - Tracing Carbon Atom Incorporation in Fatty Acids...Ch. 24 - Modeling the Regulation of AcetyI-CoA Carboxylase...Ch. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Understanding the Stoichiometry of Cholesterol...Ch. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Understanding the Mechanism of the...Ch. 24 - Prob. 13PCh. 24 - Understanding the Mechanism of the HMC-CoA...Ch. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25P
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