Stabilizing residues in protein structures are identified with Hydrophobicity Long-range interactions Conservation All of these

All of these options are correct. Stabilizing residues in protein structures are identified with hydrophobicity, long-range interactions, and conservation.

1. Hydrophobicity: Proteins fold in such a way that hydrophobic (water-hating) residues are generally found in the interior of the protein, away from water. This hydrophobic effect is a major driver of protein folding and contributes to the stability of the protein structure.

2. Long-range interactions: These are interactions between residues that are far apart in the sequence but come together in the folded protein. These can include hydrogen bonds, ionic interactions, and disulfide bonds. These interactions can significantly contribute to the stability of the protein structure.

3. Conservation: Conserved residues are those that are preserved across different species. These residues are often critical for the protein's function or structure. If a residue is conserved, it is likely contributing to the stability of the protein structure.