Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure.
نویسندگان
چکیده
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.
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عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 108 30 شماره
صفحات -
تاریخ انتشار 2011