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Detection and Characterization of Large-Scale Protein Conformational Transitions in Solution Using Charge-State Distribution Analysis in ESI-MS

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Intrinsically Disordered Protein Analysis

Part of the book series: Methods in Molecular Biology ((MIMB,volume 896))

Abstract

Ion charge-state distribution analysis in electro-spray ionization mass spectrometry (ESI-MS) is a robust and fast technique for direct detection and characterization of coexisting protein conformations in solution. Compact folded proteins give rise to ESI-generated ions carrying a relatively small number of charges, whereas less compact conformers accommodate upon ESI a larger number of charges depending on the extent of their unfolding. A chemometric approach [1] based upon factor analysis is applied to determine contributions from individual conformers to the overall CSD. Here we present basic guidelines for the use of this MS-based technique: from the preparation of suitable solutions for ESI-MS to the acquisition of reliable MS data and their subsequent analysis.

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Acknowledgements

This work was supported by a grant CHE-0750389 from the National Science Foundation.

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Correspondence to Igor A. Kaltashov .

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© 2012 Springer Science+Business Media New York

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Abzalimov, R.R., Frimpong, A.K., Kaltashov, I.A. (2012). Detection and Characterization of Large-Scale Protein Conformational Transitions in Solution Using Charge-State Distribution Analysis in ESI-MS. In: Uversky, V., Dunker, A. (eds) Intrinsically Disordered Protein Analysis. Methods in Molecular Biology, vol 896. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3704-8_24

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  • DOI: https://doi.org/10.1007/978-1-4614-3704-8_24

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  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4614-3703-1

  • Online ISBN: 978-1-4614-3704-8

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