Femtosecond laser vaporization that preserves protein-folded structure: An unproven idea

Electrospray ionization (ESI) made the transfer of nonvolatile molecules, such as proteins, from solution into the gas phase without covalent bond dissociation possible, revolutionizing MS for biological applications. However, whether the gaseous ions from ESI can preserve their biologically active native structure for characterization by MS is still controversial. The method described in ref. 1 claimed this preservation using femtosecond laser pulses to vaporize native proteins from solution into the electrospray plume used for conventional ESI/MS; the low net charge value measured for the resulting molecular ions was used as preservation evidence. Instead, however, charge value data has only been used to indicate protein conformation in solution before ESI, … [↵][1]1To whom correspondence should be addressed. E-mail: fwm5{at}cornell.edu. [1]: #xref-corresp-1-1