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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Similar questions

Five amino acids were subjected to normal phase chromatography, and the folowing Rf values were computed: A 0.59 В - 0.12 C- 0.71 D- 0.33 E - 0.20 Which is the most polar amino acid? O A O B
To which of the proteins does peak 4 correspond to? PLEASE EXPLAIN WHY A. A B. B C. C D. D E. B and C
A protein has molecular mass of 200 kDa when measured by gel filtration. When subjected to SDS PAGE with and without 2-mercaptoethanol (2-ME) the gel shown below was obtained. What is the likely subunit composition of this protein and why? a. The protein has 4 subunits, with molecular masses 100, 50, 25, and 25 kDa. 25 kDa subunits are linked to each other via noncovalent interactions. b. The protein has 4 subunits, with molecular masses 100, 50, 25, and 25 kDa. 50 kDa subunit is linked to the one 25 kDa subunit via noncovalent interactions. c. The protein has 3 subunits, with molecular masses 100, 75 and 25 kDa that are linked by noncovalent interactions. d. The protein has 4 subunits, with molecular masses 100, 75, 50 and 25 kDa. The subunits are linked by disulfide bonds. e. The protein has 4 subunits, with molecular masses 100, 50, 25, and 25 kDa. 50 kDa subunit is linked to the one 25 kDa subunit by disulfide bonds.
A mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by anion exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2 ? v First 1. Alanine v Second 2. Glutamic Acid v Third 3. Glycine 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation
42 please do not reject
(a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M 60 113588 65 Temp. (°C) 70 75 80 Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? • To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? ● Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? • Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?
1
5
You are studying a protein-protein interaction in 2 proteins. You decide to test both these proteins in different buffers and see if the interaction is preserved. You run the assay in the following buffers, pH 7.4, pH 7.4 with BME, pH 4.5, pH 3.5, pH 11, pH 12.5. The SDS gels from the assays are attached. a. What type of protein-protein interaction do these results suggest? b. What amino acids are most likely involved in this interaction? (Guess based on assay)
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?
Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.
You are studying a protein-protein interaction in 2 proteins. You decide to test both these proteins in different buffers and see if the interaction is preserved. You run the assay in the following buffers, pH 7.4, pH 7.4 with BME, pH 4.5, pH 3.5, pH 11, pH 12.5. The SDS gels from the assays are attached. a. What type of protein-protein interaction do these results suggest? b. What amino acids are most likely involved in this interaction?

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