. The process of a protein folding from an inactive unfolded structure to theactive folded structure can be represented by the following equation:unfolded protein = folded proteinThe values of AH and AS° for the folding of the protein lysozyme are:AH = -280 kJ/molAS = -790 J/mol · K(a) Calculate the value of AG for the folding of lysozyme at 25 °C.(b) At what temperature would you expect the unfolding of lysozyme tobecome favorable?

Amino acids interact with one another to give proteins. They require a well-defined 3D structure by…

Answered: . The process of a protein folding from…

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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detail how cation exchange chromatography works and what you would use to elute your target protein. What protein information would you need to facilitate this approach? Would you need to do any protein engineering to utilize cation exchange chromatography, justify your answer?
In the Bradford protein determination, the color of a dye changes from brown to blue when it binds to a protein. The intensity of blue color (measured by absorbance of light at a wavelength of 595nm) is proportional to protein concentration. Protein (ug) Absorbance at 595nm 0.00 0.466 9.36 0.676 18.72 0.883 28.08 1.086 37.44 1.280 Use Excel to determine the equation of the line in the format of y = mx + b. (I tried y=0.0218x+0.4706 and it was wrong) Using the calibration curve for the Bradford protein determination in the previous question, determine the number of micrograms of protein in an unknown if it gave an absorbance of 0.973. I tried 23.505 and it was wrong
Please solve this problem
Compute for the albumin to globulin (A/G) ratio using these data given Albumin= 51.9g/L Total protein = 75.5 g/L Note: answer should be in ratio form
Draw two reaction coordinate diagrams (DG vs reaction coordinate) that compare the uncatalyzed process of lipid flipping (lipid out à lipid in ) from outer to inner leaflet to the flippase-catalyzed process.
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
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)
Draw the product that is immediately formed when this compound reacts under the conditions described here in your template in the box labeled Problem C2. Indicate clearly whether this compound is radiolabeled by indicating the position of the labeled atom. Cells that were actively undergoing fat catabolism were isolated and bathed in a medium containing radiolabeled (13C) bicarbonate (HCO3"). Answer the questions about this specific fat remnant under these conditions. SCOA
The table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
→x D. Two physical 5. A protein unfolds according to the scheme N properties (property 1 and 2) are measured at three points in the unfolding reaction where the true values of fp are 0.2, 0.5 and 0.8. The corresponding values of K = fx/ fp are 1.0, 0.4 and 0.125. For property 1, d₁ = 0.1; for property 2, d₁ = 0.2. (a) Write an equation that can be used to calculate fapp. (b) Calculate fapp using d₁ = 0.1 (property 1) and fapp using d₁ = 0.2 (property 2). (c) The error in measurement of each physical property is 5 %. Can you detect the presence of the intermediate by measuring the physical properties? Explain your answer
a) What is cross linking? Write down its advantages and disadvantages.
bo Consider a uniport system where a carrier protein transports an uncharged substance A across a cell membrane. Suppose that at a certain ratio of [A] inside to [A] outside, the AG for the transport of substance A from outside the cell to the inside, Macmillan Leaming A outside → Ainside, is 10.7 kJ/mol at 25°C. What is the ratio of the concentration of substance A inside the cell to the concentration outside? [A]inside [A]outside Choose the true statement about the transport of A under the conditions described. Because AG is positive, the ratio [A] inside/[A]outside must be less than one. Increasing [A]outside will cause AG for movement of Aoutside to Ainside to become a larger positive number. Movement of Ainside to Aoutside will be spontaneous. Decreasing the concentration of the uniport protein in the membrane will cause AG to become a smaller positive number.

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