Question

Hydrogen and ionic bonds contribute less than hydrophobic interactions to the stability of native, aqueous proteins because-

a. They are not as strong by individual bond energy comparison

b. They always tend to be buried inside the protein structure and therefore have little effect on the stability

c. When these bonds form energy has to be invested

d. The functional groups maintaining these bonds can form them as effectively in the random coil structure

e. All of the above

Answer 1

different types of weak interactions , hydrophobic interactions are particularly important in stabilising a protien conformation . Most of the net charge in free energy that occurs when weak interactions are formed with in the protien is therefore derived form increase in entropy in the surrounding aqueous solution.

any polar or charged groups in protien interior have suitable parteners for hydrogen bonding or ionic interactions. On e hydrogen bond makes a small apparent contribution to the stability of native structure, but a presence of single hydrogen bonding group without a partner in the hydrophobic core of a protine can be so destabilising the conformations containing such a group are often thermodynamically untenable.