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Mass Spectrometry

Mass spectrometry measures molecules by mass-to-charge ratio, enabling high-resolution protein identification, quantification, post-translational modification analysis, biomarker discovery, and systems-level proteomics.

Mass Spectrometry Research

Research Overview

Mass spectrometry is one of the central technologies of modern proteomics. By converting molecules into ions and measuring their mass-to-charge patterns, researchers can identify proteins, quantify peptide abundance, detect post-translational modifications, and compare molecular signatures across biological and clinical samples.

At PanorOmics, mass spectrometry is presented as a core proteomics research technology: a bridge between protein measurement, pathway activity, biomarker discovery, clinical translation, and multi-omics interpretation.

Core Research Areas

Protein Quantification

Measuring protein abundance across samples, tissues, disease states, treatments, and biological conditions.

Peptide and Protein Identification

Identifying proteins by measuring peptide mass, fragmentation patterns, and sequence-informative spectra.

Post-translational Modification Analysis

Detecting protein modifications such as phosphorylation, acetylation, ubiquitination, glycosylation, and methylation.

Clinical Mass Spectrometry

Applying mass spectrometry to translational research, biomarker discovery, diagnostics, and precision medicine studies.

Mass Spectrometry Technologies

LC-MS/MS

Liquid chromatography coupled with tandem mass spectrometry for high-resolution peptide and protein analysis.

MALDI-TOF

Matrix-assisted laser desorption ionization time-of-flight mass spectrometry used for rapid mass measurement and protein profiling.

Orbitrap Mass Spectrometry

High-resolution mass analysis widely used in modern proteomics for accurate peptide identification and quantification.

Time-of-Flight Mass Spectrometry

Mass analysis based on ion flight time, used in proteomics, metabolomics, clinical testing, and biomolecular profiling.

Targeted Mass Spectrometry

Focused approaches such as SRM, MRM, and PRM used to measure selected proteins or peptides with high reproducibility.

Mass Spectrometry Modalities

Discovery Proteomics

Unbiased mass spectrometry profiling used to identify proteins and molecular signatures across biological samples.

Targeted Proteomics

Focused measurement of predefined proteins or peptides for validation, quantification, and translational studies.

Label-free Quantification

Compares protein abundance across samples without chemical or isotopic labeling.

Isobaric Labeling

Uses labeling strategies such as TMT or iTRAQ to compare multiple samples in multiplexed proteomics experiments.

Phosphoproteomics

Measures phosphorylation events to study signaling pathways, kinase activity, and disease-associated regulation.

Proteogenomics

Integrates mass spectrometry data with genomic and transcriptomic information to improve protein annotation and discovery.

Related proteomic approaches such as protein identification, protein interaction analysis, and biomarker discovery are explored across the Proteomics Research Center.

Landmark Mass Spectrometry Milestones

1910s–1920s

Mass Spectrometry Foundations

Early mass spectrometry established the principle of separating ions by mass-to-charge ratio.

1980s

Soft Ionization Methods

Ionization advances made it possible to analyze larger biomolecules, helping move mass spectrometry toward biological research.

1990s–2000s

Proteomics Mass Spectrometry

Mass spectrometry became central to large-scale protein identification, peptide sequencing, and proteome analysis.

2000s–Present

LC-MS/MS Proteomics

Liquid chromatography tandem mass spectrometry enabled high-throughput protein identification and quantitative proteomics.

2010s–Present

Targeted and Quantitative Proteomics

Targeted mass spectrometry strengthened reproducible protein measurement for biomarker validation and translational studies.

2015–Present

Single-cell and Ultra-sensitive Proteomics

Improved instrumentation and workflows expanded proteomics toward lower-input samples, rare cell populations, and single-cell analysis.

Present

AI-Assisted Mass Spectrometry

AI increasingly supports spectral interpretation, peptide identification, protein quantification, and proteomic signature discovery.

Featured Publications

Mass Spectrometry-Based Proteomics

Aebersold & Mann
Nature • 2003

Proteomics by Mass Spectrometry

Mann, Hendrickson & Pandey
Annual Review of Biochemistry • 2001

The Proteome: A New Concept in Protein Analysis

Wilkins et al.
Biotechnology and Genetic Engineering Reviews • 1996

Quantitative Proteomics Using Mass Spectrometry

Quantitative proteomics studies
Nature Biotechnology / Molecular & Cellular Proteomics

Targeted Mass Spectrometry for Proteomics

Targeted proteomics studies
Nature Methods / Clinical Chemistry

Deep Learning for Proteomics and Mass Spectrometry

Computational proteomics studies
Nature Methods / Nature Biotechnology
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