Given the following Hill Plot, what is the Kp for the last binding site?log 1-YO-152.52.50-2.557316-2.50.00316-2.50log[L]2.55

Kd is dissociation constant and used to express the affinity of a protein for a ligand. A lower…

Answered: Given the following Hill Plot, what is…

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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You have discovered a new hemoglobin variant you are calling Hb-21. You have noticed the following from your studies of Hb-21: - The binding constant of Hb-21 is the same at pH 7.1 and 7.4.- The binding constant curves generated by Hb-21 and O2 are sigmoidal.- The Hill coefficient for Hb-21 is 3.-The binding constant for Hb-21 with O2 in the presence of 5mM 2,3-bisphosphglycerate is about 6-times lower instead of the 8-times lower that is observed under these conditions for the wild type enzyme. Use this information to answer questions: Based on this information which of these features of hemoglobin would you conclude are altered in Hb-21 as compared to the wild type hemoglobin? ____ the cooperativity.____ the amount of T versus R state in the tissues. ____ the Bohr effect. What is the major issue for an individual with the Hb-21 variant? Explain exactly what aspect of hemoglobin’s function is altered.
Are all the proteins separated properly using two-dimensional (2D) gel electrophoresis? Why or why not?
Make use of the table below in answering the questions asked: Amino acid pK₁ pK₂ pK, Isoleucine 2.32 9.76 Leucine 2.32 9.74 Lysine 2.16 9.06 10.54 Tyrosine 2.20 9.21 10.46 I 1. Make sure to answer in two decimal places. What is the pl of the tripeptide ILY? 2. At pH 9.00, at which electrode will the ILY tripeptide be moving to? A. Anode B. Cathode C. The tripeptide will not move to either electrodes Make sure to show a solution or explanation for the answer.
The last residue of the protein (tail) is Tryptophan, and the first residue (head) is labeled with IAEDANS acceptor. Estimate the length of the protein (head to tail) if the efficiency of RET measures at 0.01 Please show step by step and how to get the 34.014 number
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In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?
Which of the following drugs is a less potent microsomal triglyceride transfer protein (MTP) inhibitor, which reduces cholesterol levels? O Structure 1 (IC50 = 23 nM) O BMS-200150 (IC50 = 2.2 µM) O Hybrid Structure (IC50 = 12 nM) %3! O Hit compound (IC50 = 36 µM) %3D Lomitapide (IC50 = 0.5 nM)
You are working at a major pharmaceutical company, and you have purified an engineered enzyme, and you need to determine the protein stability (kJ/mol). Accordingly, you have collected equilibrium unfolding data using the chemical denaturant urea at 20°C, pH 7.5 and I atmosphere using fluorescence spectroscopy. a) Determine the protein stability (AG [kJ/mol]) via nonlinear least squares (using the available data). b) Write the partial differential equation (i.e., general functional form, variable, constants). c) Describe what would happen to the isotherm if the temperature was increased to 25 °C. Urea [M] 0 0.25 0.5 0.75 1 1.25 1.5 2 2.25 2.5 2.75 3 3.25 3.5 3.75 4 4.25 4.5 4.75 5 FL 340nm 316 315.5 315 314.5 314 315 300 275 225 125 75 60 55 54 53 52.5 52.25 52 51.75 51.5 dG = Vdp-SdT+μA dnд + μB dng dGp = μA dnA+ μg dng A = Folded State B = Unfolded State
Calculate θ for a certain protein-ligand pair when the ligand concentration = 1 M and the Kd = 1 X 10-15 M.
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).
Suppose you have a concentration of 356ng/uL for Sample A. How many ng of protein will that be?
Explain what the meaning of these distances is (e.g., from where to where?)Crystal structure of human monocyte chemotactic protein-2

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Given the following Hill Plot, what is the Kp for the last binding site? log Y 1-Y 2.5 0 -2.5 2.5 316 -2.5 0.00316 -2.5 0 log[L] 2.5 5