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Peptide bonds adjacent to bulky hydrophobic residues (tryptophan, phenylalanine, leucine, isoleucine, and valine) significantly influence the local structure and properties of peptides and proteins. These residues drive protein folding, stabilize complexes, and can promote aggregation. Their presence affects solubility and presents challenges in chemical synthesis. Bulky hydrophobic residues are essential determinants for protein structure formation, stability, function, and technical handling during chemical synthesis. Their presence must be carefully considered both biologically (for understanding protein behavior) and chemically (for designing synthetic strategies).
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