![fraction bound th fraction unfolded 0.7 0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 [B] (M) LLLLLL 0 0.1 0.2 0.3 0.4 0.5 0.6 [B] (M) O frac](http://img.homeworklib.com/questions/377ac120-ea4c-11eb-bac9-836e4bc94f84.png?x-oss-process=image/resize,w_560)
Homework Answers
6) Graph which will show the unfolding off protein with a denaturant is- B
7) Graph which can be used to determine whether or not binding a ligand influences binding of additional ligands- C
8) Graph which can be used to hypothesize a mechanism of reversible inhibition- D
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6. Which graphs can be used to determine the amount of
chemical denaturant needed to unfold...
1. Which graphs can be used to estimate a Km for an enzymatic reaction? select all...
1. Which graphs can be used to estimate a Km for an enzymatic
reaction? select all that apply
2. Which graphs can be used to calculate an association
constant for a protein binding its ligand? select all that
apply
3. Which graphs can be used to estimate protein stability and
to understand folding thermodynamics? select all that apply
4. Which graphs can be used to estimate the equilibrium
constant for the dissociation of a protein-ligand complex? select
all that apply...
1. Which graph(s) can be used to estimate a Km for an enzymatic reaction? select all...
1. Which graph(s) can be used to estimate a Km for an
enzymatic reaction? select all that apply
2. Which graph(s) can be used to calculate an association
constant for a protein binding its ligand? select all that
apply
3. Which graph(s) can be used to estimate protein stability
and to understand folding thermodynamics? select all that
apply
4. Which graph(s) can be used to estimate the equilibrium
constant for the dissociation of a protein-ligand complex? select
all that apply...
Here are the graphs. instrument should have an absorbance reading of zero when there is no...
Here are the graphs.
instrument should have an absorbance reading of zero when there is no CuS04 present. Print copies of the graph for you and your partner to submit with your lab reports. Calculate the concentration of the unknown using the equation for the line. emros Concentration (M) Absorbance 0.5 1.005 0.3 0.704 0.617 0.25 0.1 0.291 0,05 0.131 0.513 Concentration VS Absorbance 1.2 y 2.1773x R2 0.9566 1 e4e4eeresases4s4 0.8 0.6 0.4 0.2 0.4 0.5 0.6 0.1 0.2...
5. What is the slope of the best fit line for the plot of a vs....
5. What is the slope of the best fit line for the plot of a vs. sin. What is the value of a at sine-1? How are these two values related? #1 Incline Angle 0-2° (m/s) 0.22 Time Interval (s) Displaceent (m) Average Velocity Average Acceleration 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 m/s/s 0.021 0.022 0.023 0.024 0.025 0.027 0.029 0.030 0.032 0.033 0.1 0.24 0.25 0.27 0.29 0.30 0.32 0.33 0.2 0.2 0.1 0.2 Average...
3. Make a plot of a vs. sin6 fon linear graph and draw a best fit...
3. Make a plot of a vs. sin6 fon linear graph and draw a best fit line through the data. Extend the best fit line so that it intersects the point at sin@ = 1 . #1 Incline Angle 0-2° (m/s) 0.22 Time Interval (s) Displaceent (m) Average Velocity Average Acceleration 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 m/s/s 0.021 0.022 0.023 0.024 0.025 0.027 0.029 0.030 0.032 0.033 0.1 0.24 0.25 0.27 0.29 0.30 0.32 0.33...
A group of families in which an autosomal dominant condition is present are studied to determine lod scores for poss...
A group of families in which an autosomal dominant condition is present are studied to determine lod scores for possible genetic linkage between three RFLP markers (R1, R2, and R3) and the disease gene. The chart shows lod scores at each of the recombination distances (0 values) tested RFLP θ values 0.05 0.10 0.15 0.20 0.25 0.30 0.35 0.40 R1 0.5 0.8 1.8 2.2 1.9 0.7 0.2 0.1 R2 1.1 3.1 3.8 3.0 2.1 1.0 0.8 0.1 R3 0.2 0.3...
LLI (nM) 92 The data at right describe the binding of a ligand to a protein:...
LLI (nM) 92 The data at right describe the binding of a ligand to a protein: 0.1 0.07 s [L] is the concentration of free ligand. e is the fraction of sites on the protein that are occupied by the ligand. (Note that some textbooks use terms like v or Y, instead of 6, to denote fractional saturation) 0.4 0.23 0.36 Answer parts (a) and (b) below. 0.55 1.2 (a) Which of the following graphs could be used to estimate...
Pump Curve and System Curve W = 1500 RPM 120.00 110.00 100.00 90.00 80.00 E 70.00...
Pump Curve and System Curve W = 1500 RPM 120.00 110.00 100.00 90.00 80.00 E 70.00 Efficiency % 60.00 50.00 40.00 30.00 20.00 10.00 0.00 -System Curve ---Pump Head Efficiency 0 1 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0. 9 O m3/s The operating discharge is, A)0.2 m/s B) 0.7 ms C) 0.31 ms D) 0.6 m/s The operating pump head Hpois, A)55 m B) 106 m C) 61 m D) 110 m 6. If the rotational velocity...
A member of my research group recently performed protein-ligand binding experiments. She used UV-Vis to determine...
A member of my research group recently performed protein-ligand binding experiments. She used UV-Vis to determine θ by monitoring the PLL The data she collected is provided below: 6. L mM 0.1 .0060 0.2 .0124 0.3 .0190 0.4 .0245 0.5 .0307 0.6 .0380 0.7 .0430 0.8 0481 0.9 0530 1.0 0591 40.0865 2.0 3.0 .170 4.0 227 5.0 283 7.5 10.0 .500 15.0 .640 20.0 721 30.0 .812 50.0 60.0 70.0 80.0 90.0 100 150 200 .889 .905 .917 0.927...
At pharmaceutical companies the goal of many drug discovery experiments is to find improved drugs over...
At pharmaceutical companies the goal of many drug discovery experiments is to find improved drugs over existing drugs that bind to a target protein of interest. The graph below shows how "Drug A" binds to a target protein 1. Protein-Ligand Binding Curve for "Drug A" 1 0.9 0.8 0.7 0.6 Y 0.5 0.4 0.3 0.2 0.1 0 0 10 15 20 25 30 35 40 From the graph, estimate the Kd of "Drug A" for the target protein. Report the...
1. Which graphs can be used to estimate a Km for an enzymatic
reaction? select all that apply
2. Which graphs can be used to calculate an association
constant for a protein binding its ligand? select all that
apply
3. Which graphs can be used to estimate protein stability and
to understand folding thermodynamics? select all that apply
4. Which graphs can be used to estimate the equilibrium
constant for the dissociation of a protein-ligand complex? select
all that apply...
1. Which graph(s) can be used to estimate a Km for an
enzymatic reaction? select all that apply
2. Which graph(s) can be used to calculate an association
constant for a protein binding its ligand? select all that
apply
3. Which graph(s) can be used to estimate protein stability
and to understand folding thermodynamics? select all that
apply
4. Which graph(s) can be used to estimate the equilibrium
constant for the dissociation of a protein-ligand complex? select
all that apply...
Here are the graphs.
instrument should have an absorbance reading of zero when there is no CuS04 present. Print copies of the graph for you and your partner to submit with your lab reports. Calculate the concentration of the unknown using the equation for the line. emros Concentration (M) Absorbance 0.5 1.005 0.3 0.704 0.617 0.25 0.1 0.291 0,05 0.131 0.513 Concentration VS Absorbance 1.2 y 2.1773x R2 0.9566 1 e4e4eeresases4s4 0.8 0.6 0.4 0.2 0.4 0.5 0.6 0.1 0.2...
5. What is the slope of the best fit line for the plot of a vs. sin. What is the value of a at sine-1? How are these two values related? #1 Incline Angle 0-2° (m/s) 0.22 Time Interval (s) Displaceent (m) Average Velocity Average Acceleration 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 m/s/s 0.021 0.022 0.023 0.024 0.025 0.027 0.029 0.030 0.032 0.033 0.1 0.24 0.25 0.27 0.29 0.30 0.32 0.33 0.2 0.2 0.1 0.2 Average...
3. Make a plot of a vs. sin6 fon linear graph and draw a best fit line through the data. Extend the best fit line so that it intersects the point at sin@ = 1 . #1 Incline Angle 0-2° (m/s) 0.22 Time Interval (s) Displaceent (m) Average Velocity Average Acceleration 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 m/s/s 0.021 0.022 0.023 0.024 0.025 0.027 0.029 0.030 0.032 0.033 0.1 0.24 0.25 0.27 0.29 0.30 0.32 0.33...
A group of families in which an autosomal dominant condition is present are studied to determine lod scores for possible genetic linkage between three RFLP markers (R1, R2, and R3) and the disease gene. The chart shows lod scores at each of the recombination distances (0 values) tested RFLP θ values 0.05 0.10 0.15 0.20 0.25 0.30 0.35 0.40 R1 0.5 0.8 1.8 2.2 1.9 0.7 0.2 0.1 R2 1.1 3.1 3.8 3.0 2.1 1.0 0.8 0.1 R3 0.2 0.3...
LLI (nM) 92 The data at right describe the binding of a ligand to a protein: 0.1 0.07 s [L] is the concentration of free ligand. e is the fraction of sites on the protein that are occupied by the ligand. (Note that some textbooks use terms like v or Y, instead of 6, to denote fractional saturation) 0.4 0.23 0.36 Answer parts (a) and (b) below. 0.55 1.2 (a) Which of the following graphs could be used to estimate...
Pump Curve and System Curve W = 1500 RPM 120.00 110.00 100.00 90.00 80.00 E 70.00 Efficiency % 60.00 50.00 40.00 30.00 20.00 10.00 0.00 -System Curve ---Pump Head Efficiency 0 1 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0. 9 O m3/s The operating discharge is, A)0.2 m/s B) 0.7 ms C) 0.31 ms D) 0.6 m/s The operating pump head Hpois, A)55 m B) 106 m C) 61 m D) 110 m 6. If the rotational velocity...
A member of my research group recently performed protein-ligand binding experiments. She used UV-Vis to determine θ by monitoring the PLL The data she collected is provided below: 6. L mM 0.1 .0060 0.2 .0124 0.3 .0190 0.4 .0245 0.5 .0307 0.6 .0380 0.7 .0430 0.8 0481 0.9 0530 1.0 0591 40.0865 2.0 3.0 .170 4.0 227 5.0 283 7.5 10.0 .500 15.0 .640 20.0 721 30.0 .812 50.0 60.0 70.0 80.0 90.0 100 150 200 .889 .905 .917 0.927...
At pharmaceutical companies the goal of many drug discovery experiments is to find improved drugs over existing drugs that bind to a target protein of interest. The graph below shows how "Drug A" binds to a target protein 1. Protein-Ligand Binding Curve for "Drug A" 1 0.9 0.8 0.7 0.6 Y 0.5 0.4 0.3 0.2 0.1 0 0 10 15 20 25 30 35 40 From the graph, estimate the Kd of "Drug A" for the target protein. Report the...
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