Biochemistry
6th Edition
ISBN: 9781337359573
Author: Reginald H. Garrett; Charles M. Grisham
Publisher: Cengage Learning US
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Textbook Question
Chapter 5, Problem 9P
Answers to all problems are at the end of this booh. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
Describe the Solid-Phase Chemical Synthesis of a Small Peptide
Describe the synthesis of the dipcptidc Lys-A]a by Merrifield’s solid-phase chemical method of peptide synthesis. What pit falls might be encountered if you attempted to add a Ieueine residue to Lys-A la to make a tripeptide?
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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
Extracts from the bacterium Bacillus brevis contain a peptide with antibiotic properties. This peptide forms complexes with
metal ions and seems to disrupt ion transport across the cell membranes of other bacterial species, leading to bacterial death.
The structure of the peptide has been determined from a series of observations.
(a) Complete acid hydrolysis of the peptide, followed by amino acid analysis, yielded equimolar amounts of Leu, Orn, Phe, Pro,
and Val. Orn is ornithine, an amino acid not present in proteins but present in some peptides. Orn has the structure
H
'H,N-CH,
-
CH2 CH2 CH2 -
C - COO-
NH,
(b) The molecular weight of the peptide is approximately 1,200 Da.
(c) The peptide failed to undergo hydrolysis when treated with the enzyme carboxypeptidase. This enzyme catalyzes the
hydrolysis of the carboxyl-terminal residue of a polypeptide unless the residue is Pro or the peptide does not contain a free
carboxyl group.
(d) Treatment of the intact peptide with…
At a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a
net charge of zero, but the predominant form of alanine at its pl is zwitterionic.
CH3
H,N
CH3
**
H¸N-C
H
Zwitterionic
H
Uncharged
OH
Select statements that explain why alanine is predominantly zwitterionic at its pl.
pk of alanine's amino group is more than its pl.
pk of alanine's carboxyl group is more than its pl.
PK of alanine's carboxyl group is less than its pl.
pk of alanine's amino group is less than its pl.
Correct Answer
What fraction of alanine is in the completely uncharged form at its pl?
1 in 2.2 × 107
1 in 1.6 × 10²
1 in 4680
1 in 9460
Chapter 5 Solutions
Biochemistry
Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...
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