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  • Title: A theoretical investigation into the lipid interactions of m-calpain.
    Author: Daman A, Harris F, Biswas S, Wallace J, Phoenix DA.
    Journal: Mol Cell Biochem; 2001 Jul; 223(1-2):159-63. PubMed ID: 11681718.
    Abstract:
    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, alpha-helical region. Our results could form a basis for future studies on the postulated lipid modulation of m-calpain activity.
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