Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure
نویسندگان
چکیده
منابع مشابه
Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure.
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 t...
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Amphiphilic lipids and hydrophobic proteins are vaporized at atmospheric pressure using nonresonant 70 femtosecond (fs) laser pulses followed by electrospray post-ionization prior to being transferred into a time-of-flight mass spectrometer for mass analysis. Measurements of molecules on metal and transparent dielectric surfaces indicate that vaporization occurs through a nonthermal mechanism. ...
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A nonresonant femtosecond laser pulse, with an intensity of 10(13) Wcm(-2), vaporizes proteins and biomolecules intact, regardless of molecular structure, size or electronic structure for subsequent electrospray ionization and transfer into a mass spectrometer. Rapid, direct analysis from dried sample, aqueous solution and cellular material is demonstrated at atmospheric pressure using laser el...
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Laser electrospray mass spectrometry (LEMS) is demonstrated for pharmaceutical samples at atmospheric pressure. A nonresonant, femtosecond duration laser pulse vaporizes native samples at atmospheric pressure into an electrospray plume for ionization with subsequent transfer into a time-of-flight mass spectrometer. The active ingredients in pharmaceutical tablets were detected in the presence o...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2011
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1105673108