For decades, scientists have understood proteins primarily through two defining features: their amino acid sequence and their three-dimensional structure. This framework has driven major advances in biology, biotechnology, and medicine, culminating in recent artificial intelligence tools capable of predicting protein structures with remarkable accuracy. Yet a fundamental challenge remains: even when a protein's sequence and structure are known, predicting its function, interactions, and behavior often remains difficult. An international team of researchers from Japan, Finland, Italy, and the United States now reports evidence that part of this missing information may lie in an often-overlooked component of proteins: the highly organized water surrounding them. In a study accepted for publication in Nature Communications, the team provides the first direct three-dimensional visualization of sequence-dependent hydration architectures surrounding peptide assemblies at sub-nanometer resolution using advanced three-dimensional atomic force microscopy (3D-AFM). The findings reveal that water near peptide and protein surfaces is not simply a passive solvent. Instead, it forms highly organized, multilayered structures whose organization is dictated by the underlying amino acid sequence and surface chemistry. These hydration architectures extend multiple layers from the peptide surface and contain distinct structural signatures associated with hydrophobic, polar, aromatic, and charged amino acid residues.