An Automated Peak Identification/Calibration Procedure forHigh‐Dimensional Protein Measures From Mass Spectrometers
Open Access
- 1 January 2000
- journal article
- research article
- Published by Wiley in BioMed Research International
- Vol. 2003 (4) , 242-248
- https://doi.org/10.1155/s111072430320927x
Abstract
Discovery of “signature” protein profiles that distinguish disease states (eg, malignant, benign, and normal) is a key step towards translating recent advancements in proteomic technologies into clinical utilities. Protein data generated from mass spectrometers are, however, large in size and have complex features due to complexities in both biological specimens and interfering biochemical/physical processes of the measurement procedure. Making sense out of such high-dimensional complex data is challenging and necessitates the use of a systematic data analytic strategy. We propose here a data processing strategy for two major issues in the analysis of such mass-spectrometry-generated proteomic data: (1) separation of protein “signals” from background “noise” in protein intensity measurements and (2) calibration of protein mass/charge measurements across samples. We illustrate the two issues and the utility of the proposed strategy using data from a prostate cancer biomarker discovery project as an example.Keywords
Funding Information
- National Cancer Institute (U01-CA86368)
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