A Conformation-Specific Approach to Native Top-down Mass Spectrometry.

Autor:	Britt HM; Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom., Ben-Younis A; Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom., Page N; Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.; LGC Group, Teddington TW11 0LY, United Kingdom., Thalassinos K; Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom.; Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, United Kingdom.
Jazyk:	angličtina
Zdroj:	Journal of the American Society for Mass Spectrometry [J Am Soc Mass Spectrom] 2024 Dec 04; Vol. 35 (12), pp. 3203-3213. Date of Electronic Publication: 2024 Oct 25.
DOI:	10.1021/jasms.4c00361
Abstrakt:	Native top-down mass spectrometry is a powerful approach for characterizing proteoforms and has recently been applied to provide similarly powerful insights into protein conformation. Current approaches, however, are limited such that structural insights can only be obtained for the entire conformational landscape in bulk or without any direct conformational measurement. We report a new ion-mobility-enabled method for performing native top-down MS in a conformation-specific manner. Our approach identified conformation-linked differences in backbone dissociation for the model protein calmodulin, which simultaneously informs upon proteoform variations and provides structural insights. We also illustrate that our method can be applied to protein-ligand complexes, either to identify components or to probe ligand-induced structural changes.
Databáze:	MEDLINE
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