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Related Concept Videos

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...
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 Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...

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Related Experiment Video

Updated: May 31, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
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Published on: June 15, 2018

Sequencing cyclic peptides by multistage mass spectrometry.

Hosein Mohimani1, Yu-Liang Yang, Wei-Ting Liu

  • 1Department of Electrical and Computer Engineering, UC San Diego, CA, USA.

Proteomics
|July 14, 2011
PubMed
Summary

This study introduces a novel multistage mass spectrometry (MS) method for sequencing cyclic peptides. This technique offers advantages over single-stage MS, enabling accurate analysis of these complex molecules with minimal material.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Analytical Chemistry
  • Computational Biology

Background:

  • Many effective antibiotics, such as Vancomycin and Daptomycin, are cyclic peptides synthesized via non-ribosomal pathways.
  • Current computational methods for sequencing cyclic peptides are underdeveloped, limiting research and drug discovery.
  • Traditional sequencing methods, like Nuclear Magnetic Resonance (NMR) spectroscopy, require large sample quantities (milligrams) that are often unattainable.

Purpose of the Study:

  • To develop an advanced computational method for sequencing cyclic peptides.
  • To demonstrate the efficacy of multistage mass spectrometry (MS) for cyclic peptide sequencing.
  • To highlight the advantages of the new method over existing single-stage MS techniques.

Main Methods:

  • Development of a novel sequencing algorithm utilizing multistage mass spectrometry (MS).
  • Application of the developed method to analyze known and novel cyclic peptides.
  • Comparative analysis of multistage MS against single-stage MS for cyclic peptide sequencing.

Main Results:

  • The developed multistage MS method successfully sequenced various cyclic peptides.
  • The technique demonstrated superior performance compared to single-stage MS.
  • The method was validated on peptides from diverse sources, including bacteria and plants.

Conclusions:

  • Multistage MS provides a powerful and sensitive approach for cyclic peptide sequencing.
  • This method significantly advances the field, enabling analysis with picograms of material.
  • The technique has broad applicability for characterizing cyclic peptides from various biological origins.