Mass Spectrometry-Based Structural Analysis of Cysteine-Rich Metal-Binding Sites in Proteins with MetaOdysseus R Software
Alternative metrics PlumXhttp://hdl.handle.net/11012/195634
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Identification of metal-binding sites in proteins and understanding metalcoupled protein folding mechanisms are aspects of high importance for the structure-tofunction relationship. Mass spectrometry (MS) has brought a powerful adjunct perspective to structural biology, obtaining from metal-to-protein stoichiometry to quaternary structure information. Currently, the different experimental and/or instrumental setups usually require the use of multiple data analysis software, and in some cases, they lack some of the main data analysis steps (MS processing, scoring, identification). Here, we present a comprehensive data analysis pipeline that addresses charge-state deconvolution, statistical scoring, and mass assignment for native MS, bottom-up, and native top-down with emphasis on metalprotein complexes. We have evaluated all of the approaches using assemblies of increasing complexity, including free and chemically labeled proteins, from low- to high-resolution MS. In all cases, the results have been compared with common software and proved how MetaOdysseus outperformed them.
Document typePeer reviewed
Document versionFinal PDF
SourceJOURNAL OF PROTEOME RESEARCH. p. -.
- Chytré nanonástroje