title: Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure.
abstract: Femtosecond laser vaporization-based mass spectrometry can be used to measure protein conformation in vitro at atmospheric pressure. Cytochrome c and lysozyme are vaporized from the condensed phase into the gas phase intact when exposed to an intense (10(13) W/cm(2)), nonresonant (800 nm), ultrafast (75 fs) laser pulse. Electrospray postionization time-of-flight mass spectrometry reveals that the vaporized protein maintains the solution-phase conformation through measurement of the charge-state distribution and the collision-induced dissociation channels.
authors: Department of Chemistry, Temple University, Philadelphia, PA 19122, USA.
authors: John J
authors: JJ
authors: Brady
authors: Elizabeth J
authors: EJ
authors: Judge
authors: Robert J
authors: RJ
authors: Levis
mesh_terms: D000818:Animals; D002645:Chickens; D045304:Cytochromes c / Q000737:chemistry; D006736:Horses; D007834:Lasers; D009113:Muramidase / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014835:Volatilization; D014867:Water
chemical_list: D011506:Proteins; D012996:Solutions; D014867:Water; D045304:Cytochromes c; D009113:Muramidase