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Katyanochek1 [597]
3 years ago
10

Assume that some protein molecule, in its folded native state, has one favored conformation. But when it is denatured, it become

s a "random coil", with many possible conformations.
How will the contribution of ΔS for native → denatured affect the favorability of the process? What apparent requirement does this impose on ΔH if proteins are to be stable structures?
Chemistry
1 answer:
san4es73 [151]3 years ago
3 0

Answer:

Gibbs Free Energy is given by the next equation: ΔG = ΔH - TΔS, where

ΔH - <u>change</u> in enthalpy

T - temperature in Kelvin

ΔS - <u>change</u> in entropy

ΔG can be:

  • ΔG>0 positive(not spontaneous reaction)
  • ΔG<0 negative(spontaneous reaction)
  • ΔG=0(in equilibrium).

→ When the proteins are denatured, the entropy of the system increases. Therefore, the ΔS also increases and becomes more positive.  

→ From the equation we see that positive value of ΔS contributes to negative value of ΔG.

The proteins are stable when there is no spontaneous reaction, thus, the ΔG>0 is required. Which means that ΔH has to be large and positive to counteract the influence of ΔS.

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For the given chemical reaction:

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The half cell reactions for the above reaction follows:

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As, aluminium is loosing 3 electrons to form aluminium cation. Thus, it is getting oxidized. Iron is gaining 2 electrons to form iron anion. Thus, it is getting reduced.

Hence, the oxidized species of the given reaction is aluminium.

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