Biology, 18.02.2020 23:32 cthompson1107
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
Answers: 2
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