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Int. J. Mol. Sci. 2017, 18(5), 913; doi:10.3390/ijms18050913

Residue Modification and Mass Spectrometry for the Investigation of Structural and Metalation Properties of Metallothionein and Cysteine-Rich Proteins

Department of Chemistry, The University of Western Ontario, London, ON N6A 3K7, Canada
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Academic Editor: Eva Freisinger
Received: 24 March 2017 / Revised: 18 April 2017 / Accepted: 20 April 2017 / Published: 26 April 2017
(This article belongs to the Special Issue Metallothioneins in Bioinorganic Chemistry: Recent Developments)
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Abstract

Structural information regarding metallothioneins (MTs) has been hard to come by due to its highly dynamic nature in the absence of metal-thiolate cluster formation and crystallization difficulties. Thus, typical spectroscopic methods for structural determination are limited in their usefulness when applied to MTs. Mass spectrometric methods have revolutionized our understanding of protein dynamics, structure, and folding. Recently, advances have been made in residue modification mass spectrometry in order to probe the hard-to-characterize structure of apo- and partially metalated MTs. By using different cysteine specific alkylation reagents, time dependent electrospray ionization mass spectrometry (ESI-MS), and step-wise “snapshot” ESI-MS, we are beginning to understand the dynamics of the conformers of apo-MT and related species. In this review we highlight recent papers that use these and similar techniques for structure elucidation and attempt to explain in a concise manner the data interpretations of these complex methods. We expect increasing resolution in our picture of the structural conformations of metal-free MTs as these techniques are more widely adopted and combined with other promising tools for structural elucidation. View Full-Text
Keywords: metallothionein structure; protein dynamics; cysteine modification; covalent labeling; ESI-MS; apo-metallothionein; metal induced protein folding metallothionein structure; protein dynamics; cysteine modification; covalent labeling; ESI-MS; apo-metallothionein; metal induced protein folding
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MDPI and ACS Style

Irvine, G.W.; Stillman, M.J. Residue Modification and Mass Spectrometry for the Investigation of Structural and Metalation Properties of Metallothionein and Cysteine-Rich Proteins. Int. J. Mol. Sci. 2017, 18, 913.

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