1.00.9Z0.815. A pharmaceutical company studied the binding ofthree different compounds, X, Y, and Z, to a particularprotein of interest. For each compound, the fractionalsaturation (v) was determined as a function ofconcentration. The results are shown in the figure.Which of the three compounds has the strongestaffinity for the protein? Explain.0.7X0.6> 0.50.40.30.20.10.0Y0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2 2.4 2.6 2.8 3.0L(μM)

Compound Z has the strongest affinity for the protein. This is indicated by the higher fractional…

Answered: 1.0 0.9 Z 0.8 15. A pharmaceutical…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The dissociation constant, Kd for a complex between protein A and protein B is 4.1 μM. If the two proteins are mixed together at initial concentrations of [A]= 0.025 μM and [B] = 4.7 μM, calculate (a) the equilibrium concentrations of A, B, and AB (the dimer formed by A and B) (b) the percentage of A bound to B
The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
When protein X is subjected to dimethylsuberimidate and SDS electrophoresis a 50 kDa band is seen; when the protein X is subjected to SDS electrophoresis without DMS, two bands of 20 kDa and 10 kDa are seen. How many different oligomeric structures of the native protein X are possible, being consistent with these observed results? one two three none of the above which is the answrr? and explain
This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
Refer to the molecular structure of Molecule 1 (attached image). This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
Hemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. 1. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer. This process is not 100% efficient, so we may have leftovers of dimers and monomers. In the graph given, can we label the peaks given as a tetramer, dimer, or monomer?
Heparin, a highly negatively charged glycosaminoglycan, is used clinically as an anticoagulant. It acts by binding several plasma proteins, including antithrombin III, an inhibitor of blood clotting. The 1:1 binding of heparin to antithrombin III seems to cause a conformational change in the protein thatgreatly increases its ability to inhibit clotting. What amino acid residues of antithrombin III are likely to interact with heparin?
An Fab fragment binds to lysozyme with a dissociation constant of Ka = 10-11 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to the Fab? [Fab] 9.9 Incorrect nM
A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0
1. Lactoferrin is an iron-binding glycoprotein that forms the antibiotic fragment lactoferricin during digestion. The protein was isolated from 1.5 liters of ewe skim milk by successive ammonium sulfate precipitation until a final salt concentration of 70% was obtained. Determine the amount (in g) of powdered ammonium sulfate needed in bringing the solution from (a) 0% to 40% saturation and (b) 40% to 70% saturation assuming that the volume remains constant. Initial concentration of (NH4)2SO4, % saturation 0 10 20 30 40 50 60 70 80 90 10 55 Final concentration of (NH4)2SO4, % saturation 30 40 50 60 70 80 Grams of solid (NH4)2SO4 to be added to 1 L of solution 176 242 314 390 472 561 657 117 405 491 584 59 421 351 438 20 113 57 182 121 61 251 325 63 188 126 195 130 65 260 337 270 202 281 135 67 210 140 70 90 761 685 511 609 533 365 292 219 146 HUGH LATLE 100 73 457 381 305 228 152 76

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