It is observed that as temperature is increased, most protein molecules go from

ID: 988428 • Letter: I

Question

It is observed that as temperature is increased, most protein molecules go from their defined, folded state into a random-coil, denatured state that exposes more hydrophobic surface area than is exposed in the folded state. Given what you have learned so far about Delta H and Delta S, explain why this is reasonable. If Delta H is negative (energy is released to break the noncovalent interactions in the folded state), the -, + situation pertains. If Delta H is positive (energy is required to break the noncovalent interactions in the folded state), the +, + situation pertains. We expect Delta S for denaturation to be negative due to the increase in conformational entropy. If Delta H is negative (energy is released to break the noncovalent interactions in the folded state), the -, - situation pertains. If Delta H is positive (energy is required to break the noncovalent interactions in the folded state), the +, - situation pertains. We expect Delta S for denaturation to be positive due to the increase in conformational entropy. Under these conditions, the denaturation process goes from being unfavorable at lower temperature to being favorable at higher temperature. Under these conditions, the denaturation process goes from being unfavorable at higher temperature to being favorable at lower temperature.

Explanation / Answer

For proteins, increase in temperature leads to unfolding of protein structure to a random coiled structure.

This is the denatured state wherein, more hydrophobic ends are now exposed.

Part A)

The above is a reasonable process as,

If dH is positive, energy is required to break the non-covalent interactions in the folded state, the +,- situation pertains.

We expect dS for denaturation to be positive due to the increase in the conformational energy

Under these conditions, the denaturation goes fom unfavorable at lower temperature to favourable at higher temperature.

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