fractional occupancy
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What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM.
- 0.01
B.0.1
C.0.91
D.0.99
- none of the listed values
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- If instead of using 3.5 µM myoglobin (receptor) you used half of this (that is, 1.75 µM myoglobin), what would be that value of the Kd, that you calculated ( how would it change)? Please explain so I can solve on my own :) (How does changing concentration of the receptor in a ligand-receptor binding experiment affect the dissociation constant?)A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
- A binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.What is the optimal substrate concentration for the enzymatic reaction presented in the Lineweaver-Burk plot below? a. -0.3211 units/mL b. –3.114 units/mL c. None of these values represent the optimal substrate concentration shown in the Lineweaver-Burk plot d. 3.114 units/mL e. 0.3211 units/mL. Studies on CAMP actions in cultured cells usually involve adding to the cell culture not CAMP, but dibutyryl CAMP (see structure). Why is this structural modification necessary? How could you test the premise that di-Bu-CAMP has the same biochemical effects as CAMP? N. N= Nat Dibutyryl CAMP O
- P CO HI F. sum21.ex1.137 Accessibility Mo 日- Which of the following molecules generally possesses a complex shape that allows the molecule to function as tools and machinery that essentially do all the work within a living cell? 15. A. triglycerides B. proteins C. carbohydrate D. A and Bare correct. 16. Which of the following molecules is NOT involved in cell-to-cell signaling? A nroctaalandine Give %00% kidomi 56°F 近 Insert F8 F6 & %24 8. K 2 G oW N M5.50 1/V, min/umol 5.00 4.50 4.00 y = 0.9474x + 2.6649 y = 0.9997x + 2.032 0.00 1.00 2.00 2.50 3.00 1/[S], uM -1 Looking at the double reciprocal plot for an enzyme in the absence of inhibitor and in the presence of two concentrations of inhibitor, what would be the Vmax for the uninhibited enzyme? (bottom graph) Equation is given. Choose the one best answer. 3.50 3.00 2.50 2.00Calculate KI' of the inhibitor from the information given. All information may not be needed to calculate. K'm = (29Ki+1.45x10^-10)/Ki Vmax = 11.7 µMs-1 Kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM Inhibitor Concentration = 5x10^-12
- 1. Start with the Michaelis-Menten equation and convert it to a double-reciprocal equation. Show how you would make a linear Lineweaver-Burk plot using this equation. 2. Based on th chart make a Lineweaver-Burk plot and later use the plot to complete the information in the table.Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.
