Characterisation of Calmodulin Structural Transitions by Ion Mobility Mass Spectrometry

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doi:10.1071/CH12047

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Characterisation of Calmodulin Structural Transitions by Ion Mobility Mass Spectrometry

Antonio N. Calabrese ^A, Lauren A. Speechley ^A and Tara L. Pukala ^A ^B

^A School of Chemistry & Physics, The University of Adelaide, Adelaide, SA 5005, Australia.
^B Corresponding author. Email: tara.pukala@adelaide.edu.au

Australian Journal of Chemistry 65(5) 504-511 http://dx.doi.org/10.1071/CH12047
Submitted: 27 January 2012 Accepted: 7 April 2012 Published: 8 May 2012





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Abstract

This study demonstrates the ability of travelling wave ion mobility-mass spectrometry to measure collision cross-sections of ions in the negative mode, using a calibration based approach. Here, negative mode ion mobility-mass spectrometry was utilised to understand structural transitions of calmodulin upon Ca²⁺ binding and complexation with model peptides melittin and the plasma membrane Ca²⁺ pump C20W peptide. Coexisting calmodulin conformers were distinguished on the basis of their mass and cross-section, and identified as relatively folded and unfolded populations, with good agreement in collision cross-section to known calmodulin geometries. Titration of calcium tartrate to physiologically relevant Ca²⁺ levels provided evidence for intermediately metalated species during the transition from apo- to holo-calmodulin, with collision cross-section measurements indicating that higher Ca²⁺ occupancy is correlated with more compact structures. The binding of two representative peptides which exemplify canonical compact (melittin) and extended (C20W) peptide-calmodulin binding models has also been interrogated by ion mobility mass spectrometry. Peptide binding to calmodulin involves intermediates with metalation states from 1–4 Ca²⁺, which demonstrate relatively collapsed structures, suggesting neither the existence of holo-calmodulin or a pre-folded calmodulin conformation is a prerequisite for binding target peptides or proteins. The biological importance of the different metal unsaturated calmodulin complexes, if any, is yet to be understood.

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