![Iructure.LUC I དང་བཅས - fraction bound fraction unfolded 0 0 0.1 0.2 0.3 0.4 05 0.6 0.7 [B] (M) 0 0.1 02 0.3 0. 40.5 0.6 0.7](http://img.homeworklib.com/questions/c594ff20-ea4c-11eb-90b3-a31c4076613e.png?x-oss-process=image/resize,w_560)
Homework Answers
1. Graph D -bgraphs can be used to estimate a Km for an enzymatic reaction
2. Graph A, C and E- graphs can be used to calculate an association constant for a protein binding its ligand
3. Graph B and F- graphs can be used to estimate protein stability and to understand folding thermodynamics
4. Graph B and F- graphs can be used to estimate the equilibrium constant for the dissociation of a protein-ligand complex
5. Graph D- graphs can be used to estimate the rate of an enzymatic reaction when the enzyme is saturated with substrate
Add Answer to:
1. Which graphs 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...
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...
6. Which graphs can be used to determine the amount of chemical denaturant needed to unfold...
6. Which graphs can be used to determine the amount of
chemical denaturant needed to unfold half of the protein molecules
in a sample? select all apply
7. Which graphs can be used to determine whether or not
binding a ligand influences binding of additional ligands? select
all that apply
8. Which graphs can be used to hypothesize a mechanism of
reversible inhibition? select all tgat apply
fraction bound th fraction unfolded 0.7 0 0.1 0.2 0.3 0.4 0.5 0.6...
Please help! 4. (3 points) Which set of binding data is likely to represent cooperative ligand...
Please help!
4. (3 points) Which set of binding data is likely to represent cooperative ligand binding to an oligomeric protein? Explain! (Note: Yor Theta is the percent saturation of receptor with ligand) a. | [Ligand] (mM) | Y 0.1 0.2 0.4 0.7 0.3 0.5 0.7 0.9 b. 0.3 0.4 0.6 0.3 0.6 0.8
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...
Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round...
Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round the answer to the 3 significant figures) 0.7 0.6 0.5 y =0.4843x+0.1951 0.4 1/v (pmol/L)/min) 0.3 30.2 0.1 0 0 0.1 0.2 0.3 0.5 0.6 0.7 0.8 0.9 0.4 1/[S] (umol/L) 2.50M 2.50 M 2.48 M 248M
thats all information i got (b) A saturated vapour of methanol and water contains 45 mol%...
thats all information i got
(b) A saturated vapour of methanol and water contains 45 mol% methanol and is to be separated using an enriching column. 250 kmol/h is fed to the bottom of the column operating at atmospheric pressure. Vapour from the top of the column is to contain 85 mol% methanol. A total condenser operates at the top of the column with a reflux ratio of 1.5 If CMO applies, determine the bottoms composition, the internal flow rates...
Use the graph to estimate K. 1.0 0.75 Yo₂ 0.5 0.25 0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 [L] (M)
Use the graph to estimate K. 1.0 0.75 Yo₂ 0.5 0.25 0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 [L] (M)
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...
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...
+0.5/1 points Previous AnswersSCalcCC4 7.2.001 2, 9x cos(Ty) is shown A direction field for the differential...
+0.5/1 points Previous AnswersSCalcCC4 7.2.001 2, 9x cos(Ty) is shown A direction field for the differential equation y y 2.0 1.5 1.0 0.5 0.4 -0.6 -0.4 -0.2 0.0 0.2 0.6 (a) Sketch the graphs of the solutions that satisfy the given initial conditions. (i) y(0) 0 (iii y(0) 1 (ii) y(0) 0.5 (iv) y(0) 1.6 V y 2:0 1.5 1.5 .5 X -0.6 O-0.6 -0.2 -0.4 0.6 -0.4 0.0 0.2 0.4 0.6 -0.2 0.0 0.2 0.4 2.0r 1.5 1.5 0.5...
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...
6. Which graphs can be used to determine the amount of
chemical denaturant needed to unfold half of the protein molecules
in a sample? select all apply
7. Which graphs can be used to determine whether or not
binding a ligand influences binding of additional ligands? select
all that apply
8. Which graphs can be used to hypothesize a mechanism of
reversible inhibition? select all tgat apply
fraction bound th fraction unfolded 0.7 0 0.1 0.2 0.3 0.4 0.5 0.6...
Please help!
4. (3 points) Which set of binding data is likely to represent cooperative ligand binding to an oligomeric protein? Explain! (Note: Yor Theta is the percent saturation of receptor with ligand) a. | [Ligand] (mM) | Y 0.1 0.2 0.4 0.7 0.3 0.5 0.7 0.9 b. 0.3 0.4 0.6 0.3 0.6 0.8
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...
Below is a Lineweaver-Burk plot of enzyme A. What is the Km of this enzyme? (round the answer to the 3 significant figures) 0.7 0.6 0.5 y =0.4843x+0.1951 0.4 1/v (pmol/L)/min) 0.3 30.2 0.1 0 0 0.1 0.2 0.3 0.5 0.6 0.7 0.8 0.9 0.4 1/[S] (umol/L) 2.50M 2.50 M 2.48 M 248M
thats all information i got
(b) A saturated vapour of methanol and water contains 45 mol% methanol and is to be separated using an enriching column. 250 kmol/h is fed to the bottom of the column operating at atmospheric pressure. Vapour from the top of the column is to contain 85 mol% methanol. A total condenser operates at the top of the column with a reflux ratio of 1.5 If CMO applies, determine the bottoms composition, the internal flow rates...
Use the graph to estimate K. 1.0 0.75 Yo₂ 0.5 0.25 0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 [L] (M)
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...
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...
+0.5/1 points Previous AnswersSCalcCC4 7.2.001 2, 9x cos(Ty) is shown A direction field for the differential equation y y 2.0 1.5 1.0 0.5 0.4 -0.6 -0.4 -0.2 0.0 0.2 0.6 (a) Sketch the graphs of the solutions that satisfy the given initial conditions. (i) y(0) 0 (iii y(0) 1 (ii) y(0) 0.5 (iv) y(0) 1.6 V y 2:0 1.5 1.5 .5 X -0.6 O-0.6 -0.2 -0.4 0.6 -0.4 0.0 0.2 0.4 0.6 -0.2 0.0 0.2 0.4 2.0r 1.5 1.5 0.5...
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