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.
Highlights
Structure is of critical importance, whether it is in the design of buildings, writing of a poem, or in the function of proteins and other macromolecules [1,2,3,4]
Nature has developed an immense catalogue of macromolecular structures that support and sustain life’s essential processes. This diversity of protein structure has necessitated the development of numerous characterization techniques each able to be applied to only certain types and sub-sets of proteins
J.sMpeolc. tSrcoi.m20e17tr, 1y8,(9I1M3 -MS), and residue modification coupled with electrospray ionization2 omf 1a9ss spectrometry (RM-MS)
Summary
Structure is of critical importance, whether it is in the design of buildings, writing of a poem, or in the function of proteins and other macromolecules [1,2,3,4]. Structure can be thought of as the position of elements within the whole, and their rigidity and other individual properties that sum together to give molecular machines and engineers amazing abilities to build skyscrapers or catalyze key reactions required for life. It is because of the inexorably linked structure/function relationship that researchers devote extraordinary efforts to determine protein structure. Nature has developed an immense catalogue of macromolecular structures that support and sustain life’s essential processes. As MTs play a role both in the proliferation of tumors and resistance to chemotherapy, much interest has been given to analytical methods to detect and quantify MTs in biological samples [60,61]
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