Shows a pronounced hydrophobic effect

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Reference no: EM13943379

Solve the following problems

Calculate the ?S for the transfer of one mole of octane to water using the change in multiplicities assumed for the first shell of water molecules surrounding the molecules.
The binding of a hydrophobic ligand to a protein also shows a pronounced hydrophobic effect. The thermodynamic data for the binding of octenoyl-CoA to the Medium chain acyl-Coa dehydrogenase(MCAD) is given below calculate ?Cp, ?S at T=308K and ?G at T=308K for this binding reaction assuming ?S at T=284K is 4.3E-2.

Temp (K)	?H (kcal/mole)
284	-9.5
288	-10.9
294	-13.3
298	-17.2
303	-19.6
308	-21.5

What do the signs for ?H, ?S and ?G tell you about the driving forces for the binding of the ligand to MCAD.
The following data was collected for a mutant version of the MCAD. Did the mutation increase or decrease the stability of the ligand binding at T=308K?

Temp (K)	?H (kcal/mole)
288	-8.0
293	-11.3
298	-13.2
303	-15.9
308	-18.7

Predict based on the Hofmeister series which of the following salts would increase the solubility of a hydrocarbon and which would decrease it: Al₂(SO₄)₃, K₃citrate, Mg₃(citrate)₂, CsI.
Ammonium sulfate is the salt most often used in salting out procedure of proteins. If my prep student accidentally wash it all down the drain which would be the best alternative: Al₂(SO₄)₃ or K₃citrate. Explain your reasoning.

Reference no: EM13943379

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