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Related Concept Videos

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...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

The quadrupole mass analyzer consists of four cylindrical metal rods arranged in a diamond carrying a DC voltage and a radio-frequency AC voltage. The motion of ions through the quadrupole depends on the field strength, causing only ions of a certain m/z to resonate successfully and strike the detector at a given field strength. Though the transmission rate for these analyzers is high, the exact elemental composition of the sample is not determined because of low resolution; however, they are...
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...
Matrix-Assisted Laser Desorption Ionization (MALDI)01:08

Matrix-Assisted Laser Desorption Ionization (MALDI)

Matrix-assisted laser desorption ionization (MALDI) is a powerful analytical technique used in mass spectrometry. It enables the identification and characterization of various biomolecules, including proteins, peptides, nucleic acids, and carbohydrates. MALDI is an ionization technique, widely employed in biological and medical research, as well as in fields like pharmacology and biochemistry.The analyte of interest, a biomolecule or a mixture of biomolecules, is mixed with a suitable matrix...
Rapid Identification of Pathogens01:25

Rapid Identification of Pathogens

MALDI-TOF MS has transformed clinical microbiology by offering a rapid and reliable method for pathogen identification. The traditional approach to microbial identification typically involves time-consuming culture techniques and biochemical tests, which can delay the initiation of appropriate antimicrobial therapy. MALDI-TOF MS avoids these delays by using characteristic ribosomal protein mass patterns of microbial cells, enabling accurate species-level identification within minutes.Principle...

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Quantitative proteomic analysis using a MALDI quadrupole time-of-flight mass spectrometer.

T J Griffin1, S P Gygi, B Rist

  • 1Department of Molecular Biotechnology, University of Washington, Seattle 98195-7730, USA. tgriffin@systembiology.org

Analytical Chemistry
|April 6, 2001
PubMed
Summary

This study introduces a method for quantifying complex protein mixtures using isotope-coded affinity tags and MALDI QqTOF mass spectrometry. This approach enables accurate protein identification and relative quantification in biological samples.

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Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Quantitative analysis of complex protein mixtures is crucial for understanding biological processes.
  • Accurate protein identification and relative quantification remain challenging in proteomics.

Purpose of the Study:

  • To develop and demonstrate a novel approach for quantitative analysis of complex protein mixtures.
  • To enable accurate protein identification and relative quantification using mass spectrometry.

Main Methods:

  • Proteins labeled with isotope-coded affinity tag reagents on cysteinyl residues.
  • Enzymatic digestion followed by multidimensional peptide separation.
  • Analysis using MALDI QqTOF mass spectrometry for quantification and identification.

Main Results:

  • Demonstrated effectiveness in quantifying and identifying peptides from a control protein mixture.
  • Successfully applied to comparative analysis of protein expression in Saccharomyces cerevisiae.

Conclusions:

  • The described approach provides a robust method for quantitative proteomics.
  • This technique facilitates accurate protein identification and relative abundance determination in complex biological systems.