Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 21746908.
- Also identified by DOI 10.1073/pnas.1105673108 and PMC identifier 3145716.
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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.
Medical subject headings
- Proteins