BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The hydrophobic amino acids (like the tiny drops of oil above) want to get out of water, so they all condense to the middle. This called the Hydrophobic Effect. Once this is done, the hydrogen bonding and polar groups interact to stabilize the overall 3D structure on the inside and outside of the protein.

Detailed explanation-2: -Solubility. Amino acids are generally soluble in water and insoluble in non-polar organic solvents such as hydrocarbons.

Detailed explanation-3: -hydrophobic-hydrophilic (HP) interactions happen when a protein is folding into its tertiary structure. The amino acids with hydrophobic side chains move to the core of the protein to be away from water, and the hydrophilic side chains move towards the outside of the protein because they have an affinity with water.

Detailed explanation-4: -Non-Polar Hydrophobic Amino Acids. Hydrophobic, as the name implies is hydro – water, phobic – fearing. Hydrophobic amino acids have little or no polarity in their side chains. The lack of polarity means they have no way to interact with highly polar water molecules, making them water fearing.