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The protease, m‐calpain, has been implicated in a number of pathological conditions. The enzyme is a calcium‐dependent heterodimer whose activity appears to be modulated by membrane interaction involving a segment, TAMRIL, located in domain V of the protein's small subunit. Based on a sequence analysis of m‐calpain, using DWIH and hydrophobic moment plot based methodologies, we have shown that this segment may contribute to a lipid interactive, oblique orientated, α‐helical region. Our results could form a basis for future studies on the postulated lipid modulation of m‐calpain activity.