Theoretical and experimental measurements show that in many cases, the contributions of ionic and hydrogen-bonding interactions to ΔH for protein folding are close to zero. Provide an explanation for this result. (Hint: Consider the environment in which protein folding occurs.)

The formation of favorable ionic or interactions in a protein replace interactions between solvent (water) and the ionic species (or donors and acceptors) in the state. The favorable ΔH obtained by formation of bonds in the protein is offset by the energy required to many interactions, with solvent going from the to the state.

Fill in the blanks above using the words listed below.

H-bonding

H-bond

intermolecular

restore

unfolded

folded

C-bond

break

intramolecular

C-bonding

The formation of favorable C-bond ionic or C-bonding interactions in a folded protein replace interactions between solvent (water) and the ionic species (or restore donors and acceptors) in the unfolded state. The favorable ΔH obtained by formation of H-bond in the H-bonding protein is offset by the energy required to break many interactions, with solvent going from the inter-molecular to the intramolecular state.

The answer is:

The formation of favorable intermolecular ionic or H-bonding interactions in a folded protein replace interactions between solvent (water) and the ionic species (or H-bond donors and acceptors) in the unfolded state. The favorable ΔH obtained by formation of intramolecular bonds in the folded protein is offset by the energy required to break many interactions, with solvent going from the unfolded to the folded state.

Explanation:

nucleus

would be most reasonable answer tbh