Bridging Native and Intrinsic Structures of Microhydrated Biomolecules by Cryogenic Ion Spectroscopy

Over the years, cryogenic ion spectroscopy has established itself as a powerful technique for studying the structures and properties of biomolecules in the gas phase. However, the transition from native environments in solution to the gas phase can lead to significant changes in the structure and properties of biomolecules. To bridge the gap between native structures in solution and intrinsic structures in the gas phase, microhydration with a controlled number of water molecules can be employed. In this talk, I will present an ion source capable of producing microsolvated ions, either by retaining solvent molecules during electrospray ionization or by condensing solvent molecules within a temperature-controlled ion trap and demonstrate the effect of microhydration on the structure of protonated arginine and tryptophan, as examples of small biomolecules, and on protein ubiquitin, as an example of a relatively large biomolecule.