Lehninger Principles of Biochemistry (Instructor's)
7th Edition
ISBN: 9781319117689
Author: nelson
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 12, Problem 10P
Summary Introduction
To determine: The way in which mutation in ras which leads to the formation of a Ras protein with no GTPase activity affects a cell’s response to insulin.
Introduction:
Mutation is defined as a change in the sequence of genetic material which occurs either due to a mistake in replication or changes in the environment. DNA enzymes have a property of proof reading which prevents the mistake in a
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
CH3
17. Which one of the
compounds below is the
HNO3
H2
1. NaNO2, HCI
Br₂
1. LiAlH4
major organic product
H2SO4
Ni
2. CuCN, KCN
FeBr3
2. H₂O, H+
obtained from the following
series of reactions?
CH3
toluene
CH3
CH3
Br
Br
Br
CH3
CH3
&&
Br
Br
NH₂
A
NH₂
NH₂
B
C
NH₂
ΝΗΣ
D
E
13. Which one of the compounds below is the major organic product obtained from the
following series of reactions?
A
+ H2C=CH-CO Me
heat
(CH3)2NH
1. LiAlH4
2. H₂O
?
1,3-butadiene
OH
'N'
B
C
14. Which one of the compounds below is the
major organic product obtained from the
following series of reactions?
'N'
D
'N'
E
1. XS CH3I
'N'
2. Ag₂O
3. H₂O, A
A
B
с
D
E
N
A
NH2
NH2
B
C
H₂N.
NH₂
D
5. The five compounds above all have molecular weights close to 75 g/mol. Which
one has the highest boiling point?
6. The five compounds above all have molecular weights close to 75 g/mol. Which
one has the lowest boiling point?
E
NH₂
Chapter 12 Solutions
Lehninger Principles of Biochemistry (Instructor's)
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
- 7. A solution of aniline in diethyl ether is added to a separatory funnel. Which ONE of the following aqueous solutions will remove aniline from the ether layer (and transfer it to the aqueous layer) if it is added to the separatory funnel and the funnel is shaken? A) aqueous NH3 B) aqueous Na2CO3 C) aqueous HCl D) aqueous NaOH E) aqueous CH3COONa (sodium acetate)arrow_forward11. Which of the following choices is the best reagent to use to perform the following conversion? A) 1. LiAlH4 2. H₂O B) HCI, H₂O D) NaOH, H₂O E) Na№3 ? 'N' 'N' C) 1. CH3MgBr 2. HCI, H₂Oarrow_forwardNH2 ΝΗΣ NH₂ NH2 NH2 A OCH3 NO₂ B C D E 1. Which one of the five compounds above is the strongest base? 2. Which one of the five compounds above is the second-strongest base? (That is, which one is next-to-strongest base?) 3. Which one of the five compounds above is the weakest base? 4. Which one of the five compounds above is the second-weakest base? (That is, which one is next-to-weakest base?) NO2arrow_forward
- Draw a diagram to demonstrate 3' to 5' exonuclease activity?arrow_forward1. Write the piece of mRNA that would code for the amino acid sequence NH3 - met - tyr - cys- his- CO2. Label the 5' and 3' ends. (diagram attached) 2.arrow_forwardYou were tasked with purifying an untagged transcription factor (molecular weight 65,000Da, isoelectric point unknown) from a contaminant Protein A (molecular weight 50,000 Da, isoelectric point 5.0). You were also instructed to use the protein for crystallization studies after purification.i) In the initial purification step, which type of chromatography should you attempt? Explain your choice and specify the requirements of the buffer solution you should use. ii) Analyzing the proteins recovered from step i) using SDS-PAGE, you still observed a faint band of Protein A in addition to the transcription factor band. Given the limited time available for further purification, you must choose ONE appropriate chromatography method to maximize the chances of separating the two proteins as well as your crystallization studies. Provide a detailed explanation of your selection and the techniques/strategies you would employ to achieve this.arrow_forward
- You were given a mixture of two proteins with different isoelectric points and molecular weights:• Protein X: pI 4.2, MW 42,000• Protein Y: pI 9.8, MW 90,000Using a Tris-glycine discontinuous native gel (pH8.3) electrophoresis system with a running gel of 12%, only a single band was observed upon protein staining after electrophoresis. Explain the observed result and discuss possible factors affecting protein migration in this system.arrow_forwardThe standard cost of Product B manufactured by Oriole Company includes 3.5 units of direct materials at $5.40 per unit. During June, 27,300 units of direct materials are purchased at a cost of $5.15 per unit, and 27,300 units of direct materials are used to produce 7,600 units of Product B. (a) Compute the total materials variance and the price and quantity variances. Total materials variance Materials price variance Materials quantity variance $ (b) Compute the total materials variance and the price and quantity variances, assuming the purchase price is $6.35 and the quantity purchased and used is 26,300 units. Total materials variance Materials price variance Materials quantity variance $arrow_forwardThe pyruvate dehydrogenase complex catalyzes the oxidative decarboxylation of pyruvate to form acetyl CoA. E₁, E2, and E3 are abbreviations for the enzymes of the complex. Classify the enzyme names, prosthetic groups, and reactions as E1, E2, or E3. E₁ E2 Answer Bank E3 transfer of electrons to FAD and then to NAD+ transfer of acetyl group to coenzyme A formation of hydroxyethyl-TPP hydroxyethyl group transferred to lipoamide thiamine pyrophosphate (TPP) FAD lipoamide dihydrolipoyl transacetylase pyruvate dehydrogenase dihydrolipoyl dehydrogenasearrow_forward
- Patients with pyruvate dehydrogenase deficiency show high levels of lactic acid in the blood. However, in some cases, treatment with dichloroacetate (DCA), which inhibits the kinase associated with the pyruvate dehydrogenase complex, lowers lactic acid levels. How does DCA act to stimulate pyruvate dehydrogenase activity? DCA activates pyruvate dehydrogenase kinase. DCA increases phosphorylation levels of pyruvate dehydrogenase. DCA inhibits pyruvate dehydrogenase kinase. ODCA activates pyruvate dehydrogenase phosphatase. What does this suggest about pyruvate dehydrogenase activity in patients who respond to DCA? The pyruvate dehydrogenase complex is active only when phosphorylated by the kinase. The pyruvate dehydrogenase complex is active only in the presence of the kinase. The pyruvate dehydrogenase complex is completely inactive. The pyruvate dehydrogenase complex displays some residual activity.arrow_forwardThe reduced coenzymes generated by the citric acid cycle donate electrons in a series of reactions called the electron-transport chain. The energy from the electron-transport chain is used for oxidative phosphorylation. Which compounds donate electrons to the electron- transport chain? H₂O NADH பப NAD+ ATP ADP FADH₂ FAD Which compounds are the final products of the electron-transport chain and oxidative phosphorylation? H₂O NADH NAD+ ΠΑΤΡ Π ADP FADH₂ FAD Which compound is the final electron acceptor in the electron-transport chain? Оно NADH NAD+ ATP ADP FADH₂ FADarrow_forwardHexokinase in red blood cells has a Michaelis constant (KM) of approximately 50 μM. Because life is hard enough as it is, let's assume that hexokinase displays Michaelis-Menten kinetics. What concentration of blood glucose yields an initial velocity (V) equal to 90% of the maximal velocity (Vmax)? [glucose] = What does the calculated substrate concentration at 90% Vmax tell you if normal blood glucose levels range between approximately 3.6 and 6.1 mM? Hexokinase operates near Vmax only when glucose levels are low. Hexokinase normally operates far below Vmax. Hexokinase operates near Vmax only when glucose levels are high. Hexokinase normally operates near Vmax mMarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
An Introduction to the Human Genome | HMX Genetics; Author: Harvard University;https://www.youtube.com/watch?v=jEJp7B6u_dY;License: Standard Youtube License