Mass Spectrometry in Systems Biology - Systems Biology: Networks, Models, and Applications - page 32

identification and quantification of biomolecules in the following
sequence: separated biomolecules are introduced into mass spectrome-
ters by soft ionization (ESI or MALDI) and detected at a predetermined
scan rate in the mass range of mass analyzers (i.e., quadrupole, ion
traps, time-of-flight, ICR) with their specific mass accuracy and resolv-
ing power. Then, biomolecules are further sequenced by tandem mass
spectrometry. New generation technologies of mass spectrometry for
proteomics will increasingly address analysis of transient structures
[120]. Development of methodologies will address the necessity to
monitor multiple time points in a quantitative manner [121].
Development of MS instruments with better sensitivity and higher
mass accuracy and resolving power is required for better understand-
ing of complex biological systems. Tandem MS as well as MS n together
with biomolecule identification through database searches and stati-
stical evaluation of the results are currently a research area driven by
requirements of studies of biological systems. In this context, separation
technologies need to be improved for specific samples and quantitation
methods should provide solutions for any biological system.
Metabolomics will need efficient sample preparation protocols to take
full advantage of analytical MS. Assembly of the results from large-
scale (omics) experiments of different families of biomolecules will be
a critical step for transforming information into knowledge.
ACKNOWLEDGMENTS
The authors acknowledge support from NIH 5R01MH067880-02 and NIH RR
11823-08. The authors would like to thank Drs. Greg Cantin, Claire Delahunty,
and John Venable for critical reading of the manuscript.
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