The most hydrophobic amino acids have side chains that are nonpolar and uncharged at physiological pH.
This is true because the side chains of the most hydrophobic amino acids are nonpolar and uncharged at physiological pH, making them less likely to interact with water. Additionally, the nonpolar side chains of these amino acids tend to form large, hydrophobic interactions within the fold of the protein structure.
The first four statements are false, as they are characteristics of the most hydrophilic amino acids rather than the most hydrophobic ones.