Characterizing Protein Complexes and Mapping their Surface and Interfacial Residues in One Native Top-Down MS Experiment with FTICR

摘要

Several groups including ours have demonstrated that a significant amount of untapped information for protein structure elucidation can be obtained in a single native top-down MS experiment using Fourier transform ion cyclotron resonance (FTICR) MS, including achieving isotopic mass resolution of large complexes to obtain accurate molecular weights, sequencing, identifying mutations, ligand binding sites, identifying and quantifying subunit variants, and most importantly, the possibility of mapping the surface or flexible regions of protein complexes. Here, we further explore the prospect of using top-down FTICR MS to probe the surface or flexible residues, and even interfacial residues of protein complexes, in the hope of bridging the MS characterization of complex components, and both proteomics and structural biology in one experiment.