High-performance collision-induced dissociation of peptide ions formed by matrix-assisted laser desorption/ionization in a quadrupole ion trap mass spectrometer.
High-performance collision-induced dissociation of peptide ions formed by matrix-assisted laser desorption/ionization in a quadrupole ion trap mass spectrometer.
复制标题
在四极离子阱质谱仪中，通过基质辅助激光解吸/电离形成的肽离子的高性能碰撞诱导解离。
DOI：
10.1021/ac00109a042
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发表时间：
1995
影响因子：
7.4
通讯作者：
Cotter,RJ
中科院分区：
文献类型：
--
作者：
Doroshenko,VM;Cotter,RJ
采用改进的离子阱检测器，对基质辅助激光解吸电离（MALDI）产生的肽离子进行了高性能的碰撞诱导解离（CID）质谱研究。MALDI离子被捕获，同时增加基本的射频场，避免了需要提高氦气压力。然后通过反向-正向-反向扫描序列分离分子离子同位素簇。然后选择同位素簇内的单个物质（通常是单同位素质量）进行活化。最后，先前用于改进正常质谱中的质量校准的端盖电极上的共振激发电压的振幅的调制现在用于为产物离子提供高质量准确度。几个质子化和钠阳离子化肽的CID质谱，其特征通常是一系列的重排离子，可用于测定氨基酸序列。碰撞诱导解离（CID）1通过与惰性气体的高能碰撞增加分子和碎片离子的碎片化，增强了质谱可用的结构信息。CID在串联仪器上使用最有效，这也提供了在第一质量分析仪中从混合物中选择单一离子物质并在第二质量分析仪中记录其CID质谱的机会。串联质谱仪目前包括四扇区、12三重四极杆、3和混合4仪器，以及傅里叶变换质谱仪（FTMS）5和四极杆离子阱6，其被配置为在单个质量分析器中进行时间串联测量。对于复杂生物结构的测定，可能需要前体离子的单位质量选择、高分辨率和产物离子的准确质量分配，并且通常只能在四扇区和FTMS仪器上实现。当然，这些高性能仪器是
A modified ion trapdetector has been utilized to obtain high-performance collision-induced dissociation (CID) mass spectra of peptide ions formed by matrix-assisted laser desorption/ionization (MALDI). MALDI ions are trapped while increasing the fundamental radio frequency field, obviating the need for elevated helium gas pres-sures. Molecular ion isotopic clusters are then isolated by a reverse-forward-reverse scan sequence. A single species within the isotopic cluster (generally the monoiso-topic mass) is then selected for activation. Finally, modulation of the amplitude of the resonant excitation voltage on the end-cap electrodes, used previously to improve mass calibration in normal mass spectra, is now utilized to provide high mass accuracy for the product ions. The CID mass spectra of several protonated and sodium-cationized peptides are presented and are often characterized by a series of rearrangement ions that can be utilized in the determination of amino acid sequences.Collision-induced dissociation (CID) 1 enhances the structural information available from mass spectrometry by increasing the fragmentation of molecular and fragment ions through energetic collisions with an inert gas. CID is used most effectively on tandem instruments, which also provide the opportunity for selection of a single ionic species from a mixture in the first mass analyzer and recording of its CID mass spectrum in the second. Tandem mass spectrometers currently include four-sector, 1 2 triple-quadrupole, 3 and hybrid4 instruments, as well as Fourier transform mass spectrometers (FTMS) 5 and quadrupole ion traps6 configured to carry out tandem-in-time measurements in a single mass analyzer. For the determinationof complex biological structures, unit mass selection of precursor ions, high resolution, and accurate mass assignment of product ions may be required7 and can generally be achieved only on four-sector and FTMS instruments. These high-performance instruments are, of course, the most