3- fully folded proteins typically have polar side chains on their surfaces, where electrostatic attractions and hydrogen bonds can form between the polar group on the amino acid and the polar molecules in the solvent. in contrast, some proteins have a polar side chain in their hydrophobic interior. which of the following would not occur to accommodate an internal, polar side chain?
a) a hydrogen bond forms between two polar side chains. b) a hydrogen bond forms between a polar side chain and protein backbone. c) a hydrogen bond forms between a polar side chain and a hydrophobic side chain. d) hydrogen bonds form between polar side chains and a buried water molecule.

Option C= A hydrogen bond formed between a polar side chain and a hydrophobic side chain.

Explanation:

All three given options a, b and d have common mechanism to accommodate the polar amino acid.

A= A hydrogen bond forms between two polar side chains.

B= A hydrogen bond from between a polar side chain and protein back bone.

D =  hydrogen bond form between polar side chains and a buried water molecules.

All these are use to accommodate the polar amino acid.

While option C is not used. which is:

A hydrogen bond formed between a polar side chain and a hydrophobic side chain.

there are no statements provided but here is why:

sulfur belongs to group 16 because it can be found in nature whether it is in a free or combined state.

hope this

in 1783 cavendish was working with his hydrogen gas and found that when he burned it and condensed the vapor it was water. this was very significant since it disproved the greek theory of elements completely since water was not a simple substance but the product of two gases. it was lavoisier who hearing of the experiment gave cavendish's gas the name hydrogen ("water-producer") and added that hydrogen burned by combining with oxygen and that water was a hydrogen-oxygen combination.

explanation: