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Mass Spectrometry Course
More than 2 million students worldwide

Mass Spectrometry Course

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Master mass spectrometry from foundational physics to advanced applications in proteomics, metabolomics, and quantitative analysis. This course delivers rigorous, practical training across instrumentation, spectral interpretation, hyphenated techniques, and regulatory compliance. Whether you work in research, pharma, or environmental science, you will gain the expertise to design, execute, and troubleshoot MS workflows with confidence.

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What you will learn:

This course covers the complete landscape of modern mass spectrometry, starting with core physical principles and instrument architecture. You will learn how to select and apply ionisation techniques, operate major mass analysers, and interpret complex spectra systematically. The curriculum includes GC-MS and LC-MS hyphenated workflows, rigorous quantitative method development, and proteomics and metabolomics applications. You will also explore advanced topics such as ion mobility, MS imaging, and bioinformatics data processing. Regulatory frameworks, data integrity principles, and laboratory safety practices are integrated throughout to prepare you for real-world professional environments.

How you study in practice Mass Spectrometry Course

How you practise Mass Spectrometry Course

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Course content

8 Chapters • 39 LessonsDuration between 4 and 360 hours (you decide)

Chapter 1See details

Foundations of Mass Spectrometry

  • Lesson 1 • Units, Nomenclature, and Notation

    Standardises the vocabulary and units used throughout the course. Prevents misinterpretation of spectra and literature values.

  • Lesson 2 • History and Scope of Mass Spectrometry

    Traces the development of MS from early ion physics to modern applications. Establishes context for why each instrumental component exists.

  • Lesson 3 • Core Physical Principles

    Covers the physics of charged particles in electric and magnetic fields. Provides the quantitative basis for understanding mass separation.

  • Lesson 4 • Overview of Instrument Architecture

    Introduces the three functional blocks: ion source, mass analyser, and detector. Students map signal flow from sample introduction to data output.

Chapter 2See details

Ionisation Techniques and Sources

  • Lesson 1 • Matrix-Assisted Laser Desorption Ionisation

    Teaches MALDI matrix selection, sample preparation, and laser parameters. Connects pulsed ionisation to time-of-flight analyser compatibility.

  • Lesson 2 • Electrospray Ionisation

    Explains the electrospray process for polar, nonvolatile, and large molecules. Links spray conditions to charge state distributions observed in spectra.

  • Lesson 3 • Gas-Phase Ionisation Methods

    Covers electron ionisation and chemical ionisation for volatile analytes. Connects ionisation energy to fragmentation extent and spectral complexity.

  • Lesson 4 • Ambient and Emerging Ionisation Sources

    Surveys DESI, DART, and related open-air ionisation techniques. Highlights minimal sample preparation as a key analytical advantage.

  • Lesson 5 • Ionisation Source Selection Strategy

    Provides a decision framework for matching ionisation method to analyte properties. Reinforces all prior ionisation concepts through comparative analysis.

Chapter 3See details

Mass Analysers and Detectors

  • Lesson 1 • Time-of-Flight Analysers

    Derives flight-time equations and explains reflectron design for improved resolution. Connects TOF to MALDI and high-throughput applications.

  • Lesson 2 • Orbitrap and FT-ICR Analysers

    Explains electrostatic trapping in Orbitrap and magnetic trapping in FT-ICR. Establishes the basis for ultra-high-resolution and exact-mass measurement.

  • Lesson 3 • Ion Trap Analysers

    Covers 3D and linear ion trap trapping, isolation, and fragmentation. Links ion storage capability to MSn experiments introduced later.

  • Lesson 4 • Quadrupole Mass Filters

    Explains RF/DC voltage operation and ion stability diagrams for quadrupoles. Connects scan speed and unit resolution to routine quantitative workflows.

  • Lesson 5 • Detectors and Signal Transduction

    Covers electron multipliers, microchannel plates, and Faraday cups. Connects detector choice to sensitivity, dynamic range, and ion counting accuracy.

Chapter 4See details

Spectral Interpretation and Fragmentation

  • Lesson 1 • Functional Group Fragmentation Patterns

    Catalogues characteristic losses and fragment ions for common functional groups. Enables rapid structural hypothesis generation from unknown spectra.

  • Lesson 2 • De Novo Structure Elucidation Workflow

    Integrates isotope, exact-mass, and fragmentation data into a stepwise elucidation strategy. Prepares students for unknown compound identification tasks.

  • Lesson 3 • Isotope Patterns and Exact Mass

    Explains natural isotope abundances and their effect on spectral patterns. Connects exact-mass measurement to molecular formula determination.

  • Lesson 4 • Reading and Annotating Mass Spectra

    Teaches identification of molecular ion, base peak, and isotope clusters. Establishes a consistent annotation workflow used throughout the course.

  • Lesson 5 • Fragmentation Mechanisms

    Covers homolytic cleavage, heterolytic cleavage, and rearrangement reactions. Provides mechanistic tools for predicting and rationalising fragment ions.

Chapter 5See details

Hyphenated Techniques: Chromatography-MS

  • Lesson 1 • GC-MS Fundamentals and Interface

    Covers column selection, carrier gas, and direct capillary interface to the ion source. Links chromatographic resolution to spectral quality and identification confidence.

  • Lesson 2 • Qualitative Identification in Hyphenated MS

    Covers library searching, retention time matching, and spectral scoring for compound identification. Establishes identification confidence criteria used in regulated workflows.

  • Lesson 3 • Troubleshooting Hyphenated MS Systems

    Diagnoses common chromatographic and MS performance issues in coupled systems. Builds practical maintenance skills essential for laboratory productivity.

  • Lesson 4 • LC-MS Interface Technologies

    Explains ESI and APCI interfaces for coupling reversed-phase and HILIC columns to MS. Addresses mobile phase compatibility and ion suppression challenges.

  • Lesson 5 • Data Acquisition Modes in Hyphenated MS

    Teaches full-scan, SIM, SRM, and data-independent acquisition strategies. Connects acquisition mode selection to sensitivity and identification goals.

Chapter 6See details

Quantitative Mass Spectrometry

  • Lesson 1 • SRM and MRM Workflow Design

    Guides transition selection, collision energy optimisation, and dwell time balancing for MRM. Produces a complete quantitative method ready for validation.

  • Lesson 2 • Method Validation Parameters

    Covers accuracy, precision, LOD, LOQ, selectivity, and stability as validation parameters. Aligns validation design with internationally recognised bioanalytical guidelines.

  • Lesson 3 • Calibration Strategies and Curve Fitting

    Teaches external calibration, matrix-matched calibration, and weighted regression. Connects calibration design to accuracy across the dynamic range.

  • Lesson 4 • Internal Standards and Isotope Dilution

    Covers stable isotope-labelled internal standards and isotope dilution MS theory. Demonstrates how internal standards correct for matrix effects and recovery variability.

  • Lesson 5 • Principles of Quantitative MS

    Establishes the relationship between ion signal and analyte concentration. Introduces response factors, linearity, and the role of matrix effects.

Chapter 7See details

Proteomics and Biomolecule Analysis

  • Lesson 1 • Peptide Fragmentation and Sequence Ions

    Explains b- and y-ion series, a-ions, and neutral losses from peptide backbone cleavage. Enables manual validation of automated peptide identifications.

  • Lesson 2 • Bottom-Up Proteomics Workflow

    Teaches LC-MS/MS data acquisition, database searching, and peptide-spectrum matching. Connects peptide identifications to protein inference and false discovery control.

  • Lesson 3 • Quantitative Proteomics Strategies

    Covers label-free quantitation, SILAC, TMT, and iTRAQ approaches. Connects quantitation strategy to experimental design and statistical power.

  • Lesson 4 • Top-Down and Native MS of Proteins

    Introduces intact protein analysis, native MS, and gas-phase protein complex characterisation. Extends proteomics skills to structural and systems biology questions.

  • Lesson 5 • Protein Sample Preparation for MS

    Covers denaturation, reduction, alkylation, and enzymatic digestion strategies. Links sample preparation quality to downstream identification confidence.

Chapter 8See details

Advanced MS Techniques and Applications

  • Lesson 1 • Ion Mobility Spectrometry Coupled to MS

    Explains drift tube, travelling wave, and trapped ion mobility separation principles. Adds a collision cross-section dimension to structural characterisation workflows.

  • Lesson 2 • Mass Spectrometry Imaging

    Teaches MALDI-MSI, DESI-MSI, and SIMS for spatially resolved molecular mapping of tissues. Connects pixel-level spectra to histological and pharmacological interpretation.

  • Lesson 3 • Metabolomics and Lipidomics by MS

    Covers untargeted and targeted metabolomics workflows, lipid class annotation, and pathway mapping. Integrates MS data with bioinformatics tools for biological interpretation.

  • Lesson 4 • Environmental and Food Safety MS Applications

    Applies high-resolution MS and multi-residue methods to contaminant screening in complex matrices. Demonstrates regulatory-aligned reporting and suspect screening workflows.

  • Lesson 5 • Tandem MS and MSn Strategies

    Covers CID, HCD, ETD, and ECD fragmentation and their complementary structural information. Connects fragmentation method selection to analyte class and structural question.

Certification

Your valid completion certificate

This course is for you:

  • Analytical chemist: wants to deepen MS expertise beyond routine daily instrument operation.

  • Pharmaceutical scientist: needs validated quantitative MS methods for regulated drug analysis.

  • Environmental scientist: applies MS to contaminant screening in complex real-world matrices.

  • Graduate student: building a rigorous MS foundation to support dissertation research independently.

  • Career changer from biology: moving into proteomics or omics roles requiring MS proficiency.

  • Quality control analyst: seeking to understand the instrumentation behind the data they report.

What our students say

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