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Tandem Mass Spectrometry01:21

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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...
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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Published on: June 19, 2010

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Modern mass spectrometry-based structural proteomics.

Evgeniy V Petrotchenko1, Christoph H Borchers2

  • 1University of Victoria-Genome British Columbia Proteomics Centre, Victoria, British Columbia, Canada.

Advances in Protein Chemistry and Structural Biology
|July 3, 2014
PubMed
Summary
This summary is machine-generated.

Modern mass spectrometry advances protein structure studies. Techniques like hydrogen-deuterium exchange and cross-linking provide crucial data for protein structure modeling and understanding protein interactions.

Keywords:
Cross-linkingHydrogen–deuterium exchangeLimited proteolysisMass spectrometryPrion proteinStructural proteomicsSurface modification

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Area of Science:

  • Biochemistry and Structural Biology
  • Analytical Chemistry
  • Proteomics

Background:

  • Mass spectrometry (MS) has revolutionized the study of proteins and peptides.
  • Structural proteomics aims to elucidate protein structure and dynamics.
  • Understanding protein structure is fundamental to biological function.

Purpose of the Study:

  • To review recent advancements in mass spectrometry-based structural proteomics.
  • To highlight techniques for studying protein structure, interactions, and dynamics.
  • To showcase the application of these techniques in protein structure modeling.

Main Methods:

  • Limited proteolysis coupled with MS
  • Surface modification coupled with MS
  • Hydrogen-deuterium exchange (HDX-MS)
  • Ion mobility spectrometry coupled with MS (IMS-MS)
  • Cross-linking coupled with MS (XL-MS)

Main Results:

  • These MS-based techniques provide complementary structural information.
  • Experimental constraints derived from these methods aid in protein structure modeling.
  • Advancements enable the study of protein interactions, conformational changes, and single protein structures.

Conclusions:

  • Modern mass spectrometry offers powerful tools for structural proteomics.
  • Integrating multiple MS-based techniques enhances the depth of structural information.
  • These methods are crucial for advancing our understanding of protein structure and function.