Can you please help show how to find This answer? Proteinmfalded <==>ProteinfaldedUnder certain conditions, a specific protein has the followingthermodynamic parameters for going from the unfolded state to thefolded state:AH = + 250 kJ/mol, and TASthose conditions, the equilibrium would lie more toward+250 kJ/mol. UnderO the unfolded stateneither would predominate - the fraction oktdotal protein that's foldedwould fraction unfolded.the folded stateIt is impossible to predict the position of the equilibrium from AH andTAS.

Proteins have four levels of the structural organization including Primary, secondary,…

Answered: Protein,nfalded==> Proteinalded Under…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 4P

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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 ΔH° and ΔS° for the folding of the protein lysozyme are: ΔH ° = -280 kJ/ mol ΔS ° = -790 J/mol • K(a) Calculate the value of ΔG° for the folding of lysozyme at 25 °C.(b) At what temperature would you expect the unfolding of lysozyme tobecome favorable? (c) At what temperature would the ratio of unfolded protein to foldedprotein be 1:5?
Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.
The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations available. To a first ap- proximation, the native, folded state can be thought to have one conforma- tion. The unfolded state can be estimated to have three possible orientations about cach bond between residues. (a) For a protein of 100 residues, estimate the entropy change per mole upon denaturation. (b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C? (c) Will the fraction denatured increase or decrease with increasing temperature?
The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations avail- able. To a first approximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues. (a) For a protein of 100 residues, estimate the entropy change per mole upon denaturation. (b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C? (c) Will the fraction denatured increase or decrease with increasing temperature?
The major difference between a protein molecule in its native state and inits denatured state lies in the number of conformations available. To a firstapproximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues.(a) For a protein of 100 residues, estimate the entropy change per moleupon denaturation.(b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?(c) Will the fraction denatured increase or decrease with increasingtemperature?
Theoretical and experimental measurements show that in many cases, thecontributions of ionic and hydrogen-bonding interactions to ΔH for proteinfolding are close to zero. Provide an explanation for this result.
. Assume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a "random coil," with many possible conformations. (a) What must be the sign of AS for the change: native → denatured? (b) How will the contribution of AS for native → denatured affect the favorability of the process? What apparent requirement does this impose on AH if proteins are to be stable structures?
Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm value
Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow.
Peptides and small proteins fold spontaneously in aqueous solution at room temperature. Thus, for a small protein in water, we can say ΔG FOLD < 0. Denoting the unfolded protein as Unf and the folded protein as Fld, we can write the following equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering the transition from the unfolded state (in which there are many possible conformations) to the folded state (only one conformation), there is clearly a decrease in the entropy of the protein. However, protein folding is (correctly) described as an entropically driven process.a) Resolve this apparent paradox by identifying the enthalpy (ΔH) and entropy (−TΔS)components involved in protein…
Do you expect a Pro → Gly mutation in a surface-loop region of a globular protein to be stabilizing or destabilizing? Assume the mutant folds toa native-like conformation. Explain your answer in terms of the predictedenthalpic and entropic effects of the mutation on the ∆G for protein foldingcompared to ∆G of folding for the wild-type protein
. The process of a protein folding from an inactive unfolded structure to the active folded structure can be represented by the following equation: unfolded protein = folded protein The values of AH and AS° for the folding of the protein lysozyme are: AH = -280 kJ/mol AS = -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 to become favorable?

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