NURSING ANM AND GNM

Detailed explanation-1: -The hydrophobic effect describes the energetic preference of nonpolar molecular surfaces to interact with other nonpolar molecular surfaces and thereby to displace water molecules from the interacting surfaces. The hydrophobic effect is due to both enthalpic and entropic effects.

Detailed explanation-2: -Hydrophobic interactions describe the relations between water and hydrophobes (low water-soluble molecules). Hydrophobes are nonpolar molecules and usually have a long chain of carbons that do not interact with water molecules. The mixing of fat and water is a good example of this particular interaction.

Detailed explanation-3: -Hydrophobicity is thought to be one of the primary forces driving the folding of proteins. On average, hydrophobic residues occur preferentially in the core, whereas polar residues tend to occur at the surface of a folded protein.

Detailed explanation-4: -Hydrophobic bonds in proteins arise as a consequence of the interaction of their hydrophobic (i.e., “water-disliking") amino acids with the polar solvent, water. The hydrophobic amino acids are gly, ala, val, leu, ile, met, pro, phe, trp (see amino acid structures for reference).