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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: Jun 4, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

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

Published on: November 28, 2017

Solid-Phase Cross-Linking (SPCL): a new tool for protein structure studies.

David Paramelle1, Christine Enjalbal, Muriel Amblard

  • 1Institut des Biomolécules Max Mousseron, CNRS, Universités Montpellier 1 et 2, Montpellier, France.

Proteomics
|February 15, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces Solid-Phase Cross-Linking (SPCL), a novel method for analyzing protein modifications. SPCL simplifies mass spectrometry analysis by isolating modified peptides, improving data consistency.

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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Related Experiment Videos

Last Updated: Jun 4, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

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

Published on: November 28, 2017

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Chemical reagents are used to study protein interactions and structures.
  • Mass spectrometry (MS) analyzes peptides from digested, modified proteins, especially when other structural data are unavailable.
  • Current methods struggle to distinguish modified from unmodified peptides during MS analysis.

Purpose of the Study:

  • To develop a more direct strategy for identifying modified peptides for MS analysis.
  • To overcome the limitations of existing methods in protein modification analysis.
  • To improve the consistency and reliability of data obtained from MS-based protein studies.

Main Methods:

  • Synthesis of solid-supported cleavable monofunctional reagents and cross-linkers.
  • Reaction of these reagents with proteins.
  • Protein digestion and selective release of modified peptide fragments.
  • Analysis of released peptides using mass spectrometry (MS).

Main Results:

  • The Solid-Phase Cross-Linking (SPCL) strategy selectively isolates modified peptide fragments.
  • Analysis focuses exclusively on modified sequences, reducing noise from unmodified peptides.
  • Consistent and reliable MS data is obtained, as relevant signals are not masked.

Conclusions:

  • SPCL offers a direct and efficient approach for analyzing protein modifications.
  • This method enhances the identification of relevant modified peptides for MS analysis.
  • SPCL improves data quality and consistency in proteomics research.