You've got a solution containing 60 μM VIP (very important protein). VIP binds to its ligand L with a Kd of 0.2 mM. If the concentration of L is 1 mM, what is the concentration of VIP bound to L?
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- 12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.A binding protein binds to a ligand L with a Kd of 400 nM. How much ligand is present when Y is (a) 0.25, (b) 0.6, (c) 0.95?Three different ligands, Ligand Q, Ligand T, and Ligand W, bind to the same protein but with different affinity: The association constant (Ka) for the binding of Ligand Q to the protein is 0.033 nM-1. The fractional saturation (Y) of the protein is 0.20 when the concentration of Ligand T is 1.25 nM. The fractional saturation (Y) of the protein is 0.80 when the concentration of Ligand W is 72 nM. Given this information, Calculate Kd for the binding of each ligand to this protein. Which ligand binds with greatest affinity? Which ligand binds with the lowest affinity?
- A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…A large chaperone protein complex GroEL is approximately 16 nm in diameter. When it is dissolved in water at 300 K, estimate the average time it will take for GroEL to diffuse a distance of 500 nm (0.5 micron). The viscosity of water is 10-3 Pa*s.
- Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.The amino acid arginine ionizes according to the following scheme: NH₂ I C=N I ΝΗ Part A pl = Submit H (CH₂)3 H-N-C-COOH II HH 1 [ΠΙ ΑΣΦ H H Calculate the isoelectric point of arginine. Express your answer using three significant figures. Request Answer pk-2.17 -H* +H* wwwww NH₂ C=N ΝΗ H (CH₂)3 1 ? H H-N-C-COO- | | H H 11 H pk-8.99 -H* +H* NH₂ I C=N I ΝΗ T (CH₂)3 H H H₂N-C-COO- I H pk - 12.5 -H* +H* NH₂ C=N=H NH I (CH₂)3 H₂N-C-COO- I H IVProtein A binds to Ligand X with a Kd of 1 μM. Protein B binds to Ligand Y with a Kd of 100 nM. Which of the following statements is TRUE? A. Protein A binds Ligand X ten times tighter than Protein B binds Ligand Y B. At a sufficiently high concentration of ligand, the binding becomes irreversible C. When the concentration of Ligand X is 1 μM, 50% of Protein A is bound to ligand D. Protein B binds to Ligand Y with a Kd of 1 × 10-8 mol/L. E. When both binding reactions are at equilibrium, Protein A has more Ligand X bound than Protein B has ligand Y bound The answer is C, could you show how to get the answer? Thanks
- If several like-charged proteins are bound simultaneously to an ion exchange column, they can be separated by gradually increasing the salt concentration (applying a “gradient”). A CM-Sepharose column has three proteins bound to it: A (pI = 7.9), B (pI = 7.4), and C (pI = 8.7). At pH = 7.0, the salt concentration on the column is gradually raised from 0 to 500 mM. In what order will the proteins elute? Explain.You have purified Protein 'X' and you want to know its concentration. As we learned, you can calculate concentrations by simply measuring UV280 absorbance of protein solutions. Using a UV spectrophotometer, you measured an absorbance of 0.6. Given that Protein X has an absorptivity (or extinction coefficient) of 0.2 mL•mg-cm at 280 nm, what is the concentration of purified protein solution (assume the light path is 1 cm)? -1 O A. 3 g/mL B. 3 mg/mL OC.0.2mg/mL OD.0.2 g/mL OE. 0.6 g/mLCalculate θ for a certain protein-ligand pair when the ligand concentration = 1 M and the Kd = 1 X 10-15 M.