Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Chapter 26, Problem 14P
Interpretation Introduction
Interpretation:
The familial hypercholesterolemia and its causes should be determined.
Concept introduction:
The steroid can be defined as a
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12:20
V
0.1-
0:09.
0.08
0:07
0.06
-0.05-
0:04-
-0.03-
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4G 56%
Problem 1 of 15
Done
On the following Michaelis-Menten
plot, estimate the value of - Vmax by
1
2
dragging the line to the appropriate
value on the y-axis.
0.01
V
max
0
0.5
|||
1.5
2.5
3.5
4
ISL
12:33
CO
4G 54%
Problem 6 of 15
Submit
Using the following reaction data
points, construct a Lineweaver-Burk
plot by dragging the points to their
relevant coordinates on the graph
and drawing a line of best fit. Based
on the plot, determine the Km.
1
mM-1
1
[S]'
"
s mM-1
V
100.0
0.100
75.0
0.080
50.0
0.060
15.0
0.030
10.0
0.025
5.0
0.020
Answer:
|||
Г
V
0.1-
0:09
0:08
0:07-
-0.06
-0.05
0:04-
0:03
0:02
0:01-
Problem 2 of 15
Done
On the following Michaelis-Menten
plot, estimate the value of Kм by
dragging the point to the appropriate
value on the x-axis.
I
T
|
0
0.5
1.5
2
KM
-0:01-
|||
25
2.5
3
3.5
4
Г
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Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Prob. 3PCh. 26 - Prob. 4PCh. 26 - Prob. 5PCh. 26 - Prob. 6PCh. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
Ch. 26 - Prob. 11PCh. 26 - Prob. 12PCh. 26 - Prob. 13PCh. 26 - Prob. 14PCh. 26 - Prob. 15PCh. 26 - Prob. 16PCh. 26 - Prob. 17PCh. 26 - Prob. 18PCh. 26 - Prob. 19PCh. 26 - Prob. 20PCh. 26 - Prob. 21PCh. 26 - Prob. 22PCh. 26 - Prob. 23PCh. 26 - Prob. 24PCh. 26 - Prob. 25PCh. 26 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39P
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- 9. Sketch NMR of the following compound. Clearly label each H-atom in the molecule and where it appears in your NMR. Clearly label the splitting (coupling) pattern (singlet, doublet etc) for each set of equivalent protons. For each signal, clearly label the integration value or the number of protons represented by the signal. Brarrow_forwardPlease help with this Mass Spectrometry Question. Thank you For the mass spec. shown in the attached image, please determine and give the amino acid sequence of the pentapeptide. Show which end is the amino terminus and which is the carboxy terminus. How does one arrive at the solution?arrow_forwardDraw a tripeptide of your choosing at pH 7. Have the N-terminus on the left and the C-terminus on the right. Then: Draw a triangle around the α-carbons. Draw a box around the R-groups. Circle the atoms capable of hydrogen bonding. Highlight the atoms involved in the formation of the peptide bonds. What type of structure have you drawn? (primary, secondary, tertiary or quaternary protein structure).arrow_forward
- 2. For the flow of fluid over a flat membrane of length 10cm, determine the length-average mass transfer coefficient. The relevant properties of the system are u=0.01cm²/s, D=5 x 106 cm²/s, and v = 5.0 cm/s.arrow_forwardBackground Freezing isn't the only challenge in cryopreservation - thawing can be just as difficult. A microwave oven seems like a nice solution, since it deposits energy quickly and microwaves are non-ionizing radiation (they do not cause DNA mutation). However, water absorbs microwaves more effectively than ice does, meaning that the portion of an organ that has already melted will get warmer at a higher rate than the remaining ice – the opposite of what we want! - The transmission of radiation through a weakly absorbing material such as ice or water can be modeled by Beer's law, which assumes that the rate of absorption at a depth x is proportional to the local radiation intensity I(x) times an absorption coefficient, which is often written as μ or a or just µ). Noting that absorption decreases the intensity, we can write a differential equation a Solving the differential equation with the boundary condition on the surface being gives the relationship For a standard microwave oven…arrow_forward3. Dry air is inhaled at a rate of 10 liter/min through a trachea with a diameter of 20 mm and a length of 125 mm. The inner surface of the trachea is at a normal body temperature of 37°C and may be assumed to be saturated with water. a. Assuming steady, fully developed flow in the trachea, estimate the mass transfer convection coefficient. b. Estimate the daily water loss (liter/day) associated with evaporation in the trachea.arrow_forward
- 1. Conceptual questions a. What dimensionless group describes the relative importance of convection versus diffusion. Explain the physical basis of this group. b. For mass transfer from a flowing fluid to a reactive surface, explain how convection increases the flux of solute to the surface.arrow_forwardAssessment +1501 pts /1600 Resources Solution ? Hint Sub bo Each pictured Lewis structure is invalid. Identify the error in each case. O Macmillan Learning :0▬▬0: Answer Bank wrong electron total :0- :F======F: octet-rule violation N :0:arrow_forward[s] mM V (M/s) Uninhibited 0.333 1.65 x 107 1.05 x 107 V (M/s) x 10' Inhibitor A V (M/s) x 107 Inhibitor B 0.794 x 107 0.40 1.86 x 107 1.21 x 107 0.893 x 107 0.50 2.13 x 107 1.43 x 107 1.02 x 107 0.666 2.49 x 107 1.74 x 107 1.19 x 107 1.0 2.99 x 107 2.22 x 107 1.43 x 107 2.0 3.72 x 107 3.08 x 107 1.79 x 107arrow_forward
- For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s. a) Calculate the Ks and KM for this reaction. b) Does substrate binding achieve equilibrium or steady state?arrow_forwardAssume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?arrow_forwardAn enzyme lowers the activation energy, (AG) of a reaction from 50.0 kcal/mol to 40.0 kcal/mol. Calulate the catalytic power at 310K. (R-1.987x10 kcal/mol)arrow_forward
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