Báo cáo Y học: Domain V of m-calpain shows the potential to form an oblique-orientated a-helix, which may modulate the enzyme's activity via interactions with anionic lipid
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The activity of m-calpain, a heterodimeric, Ca2+-dependentcysteine protease appears to be modulated by membraneinteractions involving oblique-orientated a-helix formationby a segment, GTAMRILGGVI, in the protein’s smallersubunit. Here, graphical and hydrophobic moment-basedanalyses predicted that this segment may form ana-helixwith strong structural resemblance to the influenza viruspeptide, HA2, a known oblique-orientateda-helix former.
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Báo cáo Y học: Domain V of m-calpain shows the potential to form an oblique-orientated a-helix, which may modulate the enzyme’s activity via interactions with anionic lipid
Nội dung trích xuất từ tài liệu:
Báo cáo Y học: Domain V of m-calpain shows the potential to form an oblique-orientated a-helix, which may modulate the enzyme’s activity via interactions with anionic lipid
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