Biochemistry
6th Edition
ISBN: 9781337359573
Author: Reginald H. Garrett; Charles M. Grisham
Publisher: Cengage Learning US
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Textbook Question
Chapter 17, Problem 3P
Where Do the O Atoms in Organisms Come From? Name three principal inorganic sources of oxygen atoms that are commonly available in the inanimate environment and readily accessible to the biosphere.
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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
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in a peptide with antidic properties. This peptide
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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
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(c) The peptide failed to undergo hydrolysis when treated with the
Hydrolysis of the carbonyl-terminal residue of a polypeptide une
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(d) Treatment of the peptide with 1-haw-2,4-dicherer (11N1), followed by complete hydrolysis and
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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
Chapter 17 Solutions
Biochemistry
Ch. 17 - Global Carbon Dioxide Cycling Expressed as Human...Ch. 17 - Prob. 2PCh. 17 - Where Do the O Atoms in Organisms Come From? Name...Ch. 17 - How Do Catabolism and Anabolism Differ? What are...Ch. 17 - How Art the Enzymes of Metabolic Pathways...Ch. 17 - Why Do Anabolic and Catabolic Pathways Differ? Why...Ch. 17 - Prob. 7PCh. 17 - How Is Metabolism Regulated? (Integrates with...Ch. 17 - Prob. 9PCh. 17 - Prob. 10P
Ch. 17 - Which Is “Better: NMR or MS? Compare and...Ch. 17 - How Do Vitamin-Derived Coenzymes Aid Metabolism?...Ch. 17 - What Art the Features of the Series of -omes?...Ch. 17 - Prob. 14PCh. 17 - Prob. 15PCh. 17 - Prob. 16PCh. 17 - Prob. 17PCh. 17 - Prob. 18PCh. 17 - Which of the following experimental approaches is...Ch. 17 - Prob. 20P
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- 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…arrow_forwardAt 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 9460arrow_forwardHow does a voltage-gated sodium channel work? Specifically, how and why does a change in voltage trigger their opening? Please be detailedarrow_forward
- When sodium ions enter a neuron during depolarization, they trigger the opening of additional voltage-gated sodium channels nearby, creating a positive feedback loop where the influx of sodium ions further depolarizes the membrane, causing even more sodium channels to open and allowing more sodium ions to enter the cell, thus sustaining the depolarization process until the action potential peaks. But how and why exactly does the influx of sodium ions trigger more sodium channels to let in more sodium? Please explainarrow_forwardDraw the chemical structure of the tripeptide, HEL (L - amino acids), at pH = 7.0. Calculate isoelectric pointarrow_forwardCan someone draw what this would look like?arrow_forward
- Calculate the standard change in Gibbs free energy, AGrxn, for the given reaction at 25.0 °C. Consult the table of thermodynamic properties for standard Gibbs free energy of formation values. NH,Cl(s) →NH; (aq) + C1 (aq) AGrxn -7.67 Correct Answer Determine the concentration of NH+ (aq) if the change in Gibbs free energy, AGrxn, for the reaction is -9.27 kJ/mol. 6.49 [NH+] Incorrect Answer kJ/mol Marrow_forwardWhat are some topics of interest that neurotoxicologists study? For example, toxin-induced seizures, brain death, and such along those lines?arrow_forwardCould you help me with the explanation of the answer to exercise 15, chapter 1 of Lehinger Question Nombramiento de estereoisómeros con dos carbonos quirales utilizando el sistema RS(R,R)El isómero del metilfenidato (Ritalin) se utiliza para tratar el trastorno por déficit de atención con hiperactividad (TDAH).(S,S)El isómero es un antidepresivo. Identifique los dos carbonos quirales en la siguiente estructura. ¿Es este el(R,R)o el(S,S)¿isómero? Dibuja el otro isómero. Nombramiento de estereoisómeros con dos carbonos quirales utilizando el sistema RS(R,R)El isómero del metilfenidato (Ritalin) se utiliza para tratar el trastorno por déficit de atención con hiperactividad (TDAH).(S,S)El isómero es un antidepresivo.arrow_forward
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