Nonresonant femtosecond laser vaporization of aqueous protein preserves folded structure

被引：45

作者：

Brady, John J. ^{[1
]}

Judge, Elizabeth J. ^{[1
]}

Levis, Robert J. ^{[1
]}

机构：

[1] Temple Univ, Dept Chem, Ctr Adv Photon, Philadelphia, PA 19122 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2011年 / 108卷 / 30期

基金：

美国国家科学基金会;

关键词：

multiphoton; nonthermal; IONIZATION MASS-SPECTROMETRY; ABOVE-THRESHOLD IONIZATION; ELECTROSPRAY-IONIZATION; ATMOSPHERIC-PRESSURE; CYTOCHROME-C; GAS-PHASE; CONFORMATIONAL-CHANGES; DESORPTION IONIZATION; MULTILAYER BENZENE; LARGE BIOMOLECULES;

D O I：

10.1073/pnas.1105673108

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 (1013 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.

引用

页码：12217 / 12222

页数：6

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