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Investigations into the Membrane Interactions of m-Calpain Domain V
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Biophysical Journal
- Article date:
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April 1, 2005
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Copyright informationCopyright Biophysical Society Apr 2005. Provided by ProQuest LLC. (Hide copyright information)
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ABSTRACT
m-Calpain is a calcium-dependent heterodimeric protease implicated in a number of pathological conditions. The activation of m-calpain appears to be modulated by membrane interaction, which has been predicted to involve oblique-orientated α-helix formation by a GTAMRILGGVI segment located in domain V of the protein's small subunit. Here, we have investigated this prediction. Fourier transform infrared conformational analysis showed that VP1, a peptide homolog of this segment, exhibited α-helicity of ~45% in the presence of dimyristoylphosphatidylcholine/dimyristoylphosphatidylserine (DMPS) vesicles. The level of helicity was unaffected over a 1- to 8-mM concentration ...
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