Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 6, Problem 12RE
REFLECT AND APPLY Can the presence of a catalyst increase the amount of product obtained in a reaction?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
From the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant.
Time (s)
0
Reactant (mM)
5.4
1
4.6
2
3.9
3
3.2
4
2.7
5
2.3
Only a plot of In[reactant] versus t gives a straight line, so the reaction is
first order
. The negative of the slope, k, is
0.171
Hair grows at a rate of about 20 cm/yr. All this growth is concentrated at the base of the hair fiber, where a-keratin filaments are
synthesized inside living epidermal cells and assembled into ropelike structures.
Two-chan
14
Protofilament
20-30 A
Two-chain
Intermediate
flament
-Protob
Protofilament
Cross section of a hair
The fundamental structural element of a keratin is the a helix, which has 3.6 amino acid residues per turn and a rise of 5.4 A
perlum.
54A
(36)
Amino terminus
Carbon
Hydrogen
Oxygen
Nitrogen
group
Carboxyl terminus
Assuming that the biosynthesis of a helical keratin chains is the rate-limiting factor in the growth of hair, calculate the rate at
which peptide bonds of a-keratin chains must be synthesized (peptide bonds per second) to account for the observed yearly
growth of hair.
0422
rate of peptide bond formation:
Income
bonds/s
Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a
polypeptide to a random conformation is accompanied by a large decrease in specific rotation.
Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the
pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH
10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph.
a Helix
Specific rotation
Poly(Glu)
a Helix
Random
conformation
Poly(Lys)
Random conformation
T
+
°
2
4
6 В
10 12 14
PH
Complete the statements about the molecular mechanism for these changes in specific rotation.
Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue
Comed Artwer
lose a proton. The negatively charged groups in each glutamate residue…
Chapter 6 Solutions
Biochemistry
Ch. 6 - RECALL How does the catalytic effectiveness of...Ch. 6 - RECALL Are all enzymes proteins?Ch. 6 - MATHEMATICAL Catalase breaks down hydrogen...Ch. 6 - REFLECT AND APPLY Give two reasons why enzyme...Ch. 6 - RECALL For the reaction of glucose with oxygen to...Ch. 6 - REFLECT AND APPLY Would nature rely on the same...Ch. 6 - REFLECT AND APPLY Suggest a reason why heating a...Ch. 6 - REFLECT AND APPLY A model is proposed to explain...Ch. 6 - REFLECT AND APPLY Does the presence of a catalyst...Ch. 6 - REFLECT AND APPLY What effect does a catalyst have...
Ch. 6 - REFLECT AND APPLY An enzyme catalyzes the...Ch. 6 - REFLECT AND APPLY Can the presence of a catalyst...Ch. 6 - RECALL For the hypothetical reaction 3A+2B2C+3D...Ch. 6 - REFLECT AND APPLY The enzyme lactate dehydrogenase...Ch. 6 - REFLECT AND APPLY Would you use a pH meter to...Ch. 6 - REFLECT AND APPLY Suggest a reason for carrying...Ch. 6 - RECALL Distinguish between the lock-and-key and...Ch. 6 - RECALL Using an energy diagram, show why the...Ch. 6 - REFLECT AND APPLY Other things being equal, what...Ch. 6 - REFLECT AND APPLY Amino acids that are far apart...Ch. 6 - REFLECT AND APPLY If only a few of the amino acid...Ch. 6 - RECALL Show graphically how the reaction velocity...Ch. 6 - RECALL Define steady state, and comment on the...Ch. 6 - RECALL How is the turnover number of an enzyme...Ch. 6 - MATHEMATICAL For an enzyme that displays...Ch. 6 - MATHEMATICAL Determine the values of KM and Vmax...Ch. 6 - MATHEMATICAL The kinetic data in the following...Ch. 6 - MATHEMATICAL The enzyme -methylaspartase catalyzes...Ch. 6 - MATHEMATICAL The hydrolysis of a...Ch. 6 - MATHEMATICAL For the Vmax obtained in Question 26,...Ch. 6 - MATHEMATICAL You do an enzyme kinetic experiment...Ch. 6 - REFLECT AND APPLY The enzyme D-amino acid oxidase...Ch. 6 - REFLECT AND APPLY Why is it useful to plot rate...Ch. 6 - REFLECT AND APPLY Under what conditions can we...Ch. 6 - BIOCHEMICAL CONNECTIONS Why does acetazolamide...Ch. 6 - BIOCHEMICAL CONNECTIONS How did scientists...Ch. 6 - BIOCHEMICAL CONNECTIONS How do the KM values for...Ch. 6 - Prob. 38RECh. 6 - RECALL What are the three most common mechanisms...Ch. 6 - RECALL What is the biggest difference between a...Ch. 6 - RECALL How do scientists determine the KM of a...Ch. 6 - Prob. 42RECh. 6 - Prob. 43RECh. 6 - RECALL Do all enzymes display kinetics that obey...Ch. 6 - RECALL How can you recognize an enzyme that does...Ch. 6 - RECALL If we describe an enzyme like aspartate...Ch. 6 - RECALL How can competitive and pure noncompetitive...Ch. 6 - RECALL Why does a competitive inhibitor not change...Ch. 6 - RECALL Why does a pure noncompetitive inhibitor...Ch. 6 - RECALL Distinguish between the molecular...Ch. 6 - RECALL Can enzyme inhibition be reversed in all...Ch. 6 - RECALL Why is a Lineweaver-Burk plot useful in...Ch. 6 - RECALL Where do lines intersect on a...Ch. 6 - RECALL What is the difference between pure and...Ch. 6 - REFLECT AND APPLY Why can we say that having a...Ch. 6 - REFLECT AND APPLY When we compare the binding of I...Ch. 6 - RECALL Why does the apparent KM decrease in the...Ch. 6 - RECALL What is a suicide substrate? Why are they...Ch. 6 - RECALL If we made a Lineweaver-Burk plot of an...Ch. 6 - Prob. 60RECh. 6 - MATHEMATICAL For the following aspartase reaction...Ch. 6 - REFLECT AND APPLY Is it good (or bad) that enzymes...Ch. 6 - REFLECT AND APPLY Noncompetitive inhibition is a...Ch. 6 - BIOCHEMICAL CONNECTIONS You have been hired by a...Ch. 6 - REFLECT AND APPLY Would you expect an irreversible...Ch. 6 - REFLECT AND APPLY Would you expect the structure...Ch. 6 - Prob. 67RECh. 6 - Prob. 68RE
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- From the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 6.2 1 3.1 2 2.1 3 1.6 4 1.3 5 1.1 Only a plot of 1/[reactant] versus t gives a straight line, so the reaction is 0.150 mM-1 s-1 . S second order . The slope, k, isarrow_forwardFrom the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 5.4 1 4.6 2 3.9 3 3.2 4 2.7 5 2.3 Only a plot of In[reactant] versus t gives a straight line, so the reaction is s-1. . The negative of the slope, k, isarrow_forwardA protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. How many subunits does the protein have, and what is the molecular mass of each? four subunits: 180, 160, 90, and 60 kDa three subunits: 180, 160, and 60 kDa three subunits: 160, 90, and 60 kDa four subunits: 160, 90, 90, and 60 kDa Correct Answerarrow_forward
- Calculate KM and Vmax from the following data: KM= i Vmax [S] (μM) vo (mM.s-¹) 0.1 0.34 0.2 0.53 0.4 0.74 0.8 0.91 1.6 1.04 μM mM s-1arrow_forwardPropose a detailed chemical mechanism for the enzyme catalyzed reaction below and briefly note similarities, if any, to enzymes that we've studied. CO2 + CO2 2 CO2 HO CH3arrow_forwardState and describe the four stages of protein formation, please include the types of bonds at each stage.arrow_forward
- Please state and describe the four different types of non-covalent interactions.arrow_forwardPls help with these three questionsarrow_forward11. Which of the compounds below is the major product of the following reaction sequence? NOTE: PCC is pyridinium chlorochromate 1. BH 3 PCC 2. H2O2, NaOH NH HN ΗΝ, A B C CH3NH2, NaBH3CN D E NHarrow_forward
- 10. Which of the compounds below is the major organic product obtained from the following reaction sequence? Ph Ph Ph A B OH 1. EtMgBr H2CrO4 Zn(Hg), aq. HCI PhCHO ? 2. H₂O, H+ Ph. C D Ph "ར HO OH Earrow_forward7. What is the major organic product obtained from the following reaction sequence? Ph A OH 99 Ph OH D Br HOCH2CH2OH H2SO4 1. Mg, Et₂O 2. PhCH2CHO HCI, H₂O Br OH Ph Ph OH B C Br OH Ph Earrow_forwardPls helparrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY