Protein-sequence analysis provides an important route for examining the structural organization of viral proteins when sequence composition is considered together with experimentally assigned secondary-structure information. This study investigates Ebola virus proteins by segmenting amino acid sequences into overlapping triplet codes and evaluating the relative enrichment or depletion of those triplets through a normalized deviation parameter. The analysis is designed to identify triplet patterns that occur more or less frequently than expected and to compare these patterns with secondary-structure assignments derived from DSSP. Amino acid triplets are counted using a Python program, observed and expected frequencies are calculated, and the resulting deviation values are normalized to a common 0–1 scale. The same procedure is applied to triplets associated with alpha-helical, beta-sheet, and random-coil regions. The sequence-level analysis identifies several triplets with comparatively high normalized deviations, including methionine-rich and glutamine/tyrosine-containing combinations, while the structure-level analysis indicates that several enriched triplets are associated preferentially with alpha-helical regions. These results provide a descriptive statistical view of triplet usage and its relationship with protein secondary structure. The triplet-based patterns should not be interpreted as direct evidence of biochemical function or therapeutic relevance without independent structural and experimental validation. Nevertheless, the method offers a compact way to compare local amino acid context with structural preference and may complement established sequence- and structure-prediction approaches for Ebola virus proteins.
