Advances in mass spectrometry instrumentation and experimental design have led to significant inroads in the characterization of intact proteins and protein complexes, thus translating to new applications in the field of proteomics and structural biology. Ultraviolet photodissociation (UVPD) results in broad sequence coverage of intact proteins via more extensive backbone fragmentation than obtained from other ion activation methods, and ion activation/dissociation can be accomplished using a single 5 ns laser pulse. UVPD offers a frontier MS/MS technology for characterization of intact proteins, including mapping post-translational modifications and ligand binding sites. There has been growing interest in employing top-down approaches to examine native-like protein structures by using MS/MS to disassemble the complexes and sequence the constituent proteins. In the context of protein-ligand complexes, the relative abundances of fragment ions generated by UVPD correlate with variations in the intramolecular and intermolecular interactions that stabilize particular regions of the proteins. Owing to the fast, high energy deposition of UV photoactivation, products retaining non-covalently bound ligands are formed and afford binding site information. For multimeric protein complexes, UVPD disassembles the complexes to reflect sub-unit architecture as well as sequence ions that identify the proteins. <br/>

<b>Award Address</b> (Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry sponsored by the Waters Corporation). Ultraviolet photodissociation mass spectrometry for characterization of proteins and protein complexes

2019 Spring National Meeting

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Award Address (Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry sponsored by the Waters Corporation). Ultraviolet photodissociation mass spectrometry for characterization of proteins and protein complexes