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.

answer; ///(u-235); ///is the correct

adding or remove a gaseous reactant or product changes the concentrations. if the concentration of reactant or product is increased, the system will shift away from the side in which concentration was increased (i.e. if the concentration of reactants is increased, the system will shift toward the products. if more products are added, the system will shift to form more reactants). conversely, if the concentration of reactant or product is decreased, the system will shift toward the side in which concentration was decreased (i.e. if reactants are removed, the system will shift to form more reactants. if the concentration of products is decreased, the equilibrium will shift toward the products).

explanation: