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MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For example, the mass of helium...
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
Mass Spectrometers01:16

Mass Spectrometers

This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:
Mass Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...
Mass Spectrum01:23

Mass Spectrum

A mass spectrum is the graphical representation of the relative abundance of the charged fragments in an analyte plotted against their mass-to-charge ratio (m/z). The plot's x-axis represents the ratio of the mass of the charged fragment to the number of charges it carries. The y axis of the plot represents the relative abundance of each charged species. The relative abundance is calculated from the signal intensity of each charged species recorded at the detector. The most intense signal (the...

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Related Experiment Video

Updated: Jun 2, 2026

Characterization of Synthetic Polymers via Matrix Assisted Laser Desorption Ionization Time of Flight (MALDI-TOF) Mass Spectrometry
06:56

Characterization of Synthetic Polymers via Matrix Assisted Laser Desorption Ionization Time of Flight (MALDI-TOF) Mass Spectrometry

Published on: June 10, 2018

Self-calibrated warping for mass spectra alignment.

Q Peter He1, Jin Wang, James A Mobley

  • 1Department of Chemical Engineering, Tuskegee University, Tuskegee, AL 36088, USA.

Cancer Informatics
|May 10, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a novel self-calibrated warping (SCW) algorithm for aligning mass spectrometry (MS) spectra from biological fluids. The SCW algorithm improves data consistency for analyzing protein profiles in clinical samples.

Keywords:
alignmentdata preprocessingfeature extractionmass spectrometrypeak detectionproteomicswarping

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Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

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Last Updated: Jun 2, 2026

Characterization of Synthetic Polymers via Matrix Assisted Laser Desorption Ionization Time of Flight (MALDI-TOF) Mass Spectrometry
06:56

Characterization of Synthetic Polymers via Matrix Assisted Laser Desorption Ionization Time of Flight (MALDI-TOF) Mass Spectrometry

Published on: June 10, 2018

MALDI Sample Preparation: the Ultra Thin Layer Method
05:28

MALDI Sample Preparation: the Ultra Thin Layer Method

Published on: April 29, 2007

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
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Published on: January 20, 2022

Area of Science:

  • Biomarker Discovery
  • Proteomics
  • Analytical Chemistry

Background:

  • Mass spectrometry (MS) enables protein profile analysis in small biological specimens.
  • Inconsistent spectral alignment across samples hinders reliable analysis of MS data.
  • Existing alignment algorithms often fail with unique characteristics of body fluid MS data.

Purpose of the Study:

  • To develop a robust spectrum alignment algorithm for serum and body fluid MS data.
  • To address challenges specific to the alignment of mass spectrometry spectra from clinical samples.

Main Methods:

  • Proposed a novel self-calibrated warping (SCW) algorithm for MS spectrum alignment.
  • Evaluated SCW against five existing alignment methods.
  • Utilized a clinical surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) dataset for comparison.

Main Results:

  • The self-calibrated warping (SCW) algorithm demonstrates effectiveness in aligning MS spectra.
  • SCW addresses specific challenges inherent in serum and body fluid MS data.
  • Comparative analysis highlights the performance of SCW against established methods.

Conclusions:

  • The SCW algorithm offers an improved approach for mass spectrometry data alignment in clinical proteomics.
  • Enhanced spectral alignment ensures greater consistency and reliability in biomarker discovery from body fluid samples.