Charge, Color, and Conformation: Spectroscopy on Isomer-Selected Peptide Ions.

摘要: Monitoring the chromism induced by intramolecular hydrogen and charge transfers within proteins as well isomerization of both protein cofactor is essential not only to understand photoactive signaling pathways but also design targeted opto-switchable proteins. We used a dual-ion mobility drift tube coupled tunable picosecond laser explore optical structural properties peptide chain bound chromophore—a prototype system allowing for proton transfer conformational change. With support molecular dynamics DFT calculations, we show how between its can dramatically modify demonstrate that these changes be triggered collisional activation in gas phase.