Construction of a hybrid quadrupole/fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10 kDa
| Autor: | Steven M. Patrie, Jay P. Charlebois, John P. Quinn, Christopher L. Hendrickson, David Whipple, Biswarup Mukhopadhyay, Alan G. Marshall, Neil L. Kelleher |
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| Rok vydání: | 2004 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Analytical chemistry 010402 general chemistry Tandem mass spectrometry Top-down proteomics Mass spectrometry Ion cyclotron resonance spectrometry Sensitivity and Specificity 01 natural sciences Gas Chromatography-Mass Spectrometry Mass Spectrometry Fourier transform ion cyclotron resonance Bacterial Proteins Sequence Analysis Protein Structural Biology Spectroscopy Fourier Transform Infrared Infrared multiphoton dissociation Spectroscopy Electron-capture dissociation Chemistry 010401 analytical chemistry Proteins Reproducibility of Results 0104 chemical sciences Equipment Failure Analysis Equipment Failure Ion trap |
| Zdroj: | Journal of the American Society for Mass Spectrometry. 15:1099-1108 |
| ISSN: | 1044-0305 |
| DOI: | 10.1016/j.jasms.2004.04.031 |
| Popis: | Technological advancements including an open-cylindrical Penning trap with capacitively coupled ICR cell, selective ion accumulation with a resolving quadrupole, and a voltage gradient used during ion extraction from an octopole ion trap, have individually improved dynamic range and sensitivity in Fourier Transform Ion Cyclotron Resonance Mass Spectrometry (FT-ICR MS). Documented here is a new instrument utilizing these technologies toward the robust detection and fragmentation of biomolecules >10 kDa. Up to 55-fold enhancement in ion population by selective ion accumulation combined with 10- to 20- fold signal-to-noise improvement by application of a DC voltage gradient to an accumulation octopole during the ion transfer event offers improved signal-to-noise (or speed) of MS/MS experiments, for proteins from Methanococcus jannaschii and Saccharomyces cerevisiae whole cell lysates. After external quadrupole filtering with a 40 m/z window, three proteins were fragmented (and identified) in parallel from the database of Methanococcus jannaschii. Electron capture dissociation (ECD) of an intact yeast protein provides extensive sequence information resulting in a high degree of localization for an N-terminal acetylation. Hybrid fragmentation, infrared multiphoton dissociation (IRMPD) followed by low energy electrons (ECD), with the electron source located laterally off the z-axis and external to the magnet bore, presents a strategy for identification of proteins by means of the sequence tag approach. Automated implementation of diverse MSn approaches in a Q-FTMS instrument promises to help realize “top-down” proteomics in the future. |
| Databáze: | OpenAIRE |
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