LAUSR

Structural studies of mass-selected biomolecules in the gas phase can reveal their intrinsic properties and provide useful benchmarks for biomolecular modeling. Here, we report the first evidence of transition metal ion FRET (tmFRET) in the gas phase and its application to measure short (10-40 Å) biomolecular backbone distances. The measured FRET efficiencies in rhodamine dye (donor) labeled helical peptides complexed with Cu2+ ions (acceptor) decreased with increasing donor - acceptor distances, confirming the occurrence of tmFRET. The distances estimated for similar peptide sequences from the FRET efficiencies were consistently longer in the gas phase compared to those reported in solution, indicating an expanded structure and a possible loss of helicity.