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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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...
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Protein Complex Assembly02:41

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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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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Probing structures of large protein complexes using zero-length cross-linking.

Roland F Rivera-Santiago1, Sira Sriswasdi2, Sandra L Harper3

  • 1The Center for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, PA 19104, United States; Biochemistry and Molecular Biophysics Graduate Group, University of Pennsylvania, Philadelphia, PA 19104, United States.

Methods (San Diego, Calif.)
|May 5, 2015
PubMed
Summary
This summary is machine-generated.

Structural mass spectrometry (MS) advances "zero-length" cross-linking for precise protein interaction analysis. New methods improve identification of cross-linked peptides, refining molecular models.

Keywords:
Chemical cross-linkingCross-link identificationMass spectrometryMolecular modelingStructureZero-length cross-linking

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Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
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Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
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Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

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Area of Science:

  • Biophysics
  • Structural Biology
  • Analytical Chemistry

Background:

  • Structural mass spectrometry (MS) is crucial for studying protein complexes.
  • Chemical cross-linking coupled with MS (CX-MS) identifies proximal sites in macromolecules.
  • Cross-linked sites reveal protein-protein interactions and refine molecular models.

Purpose of the Study:

  • This review focuses on recent advances in "zero-length" cross-linking techniques.
  • Highlights the advantages of zero-length cross-linking for precise distance constraints.
  • Addresses challenges in identifying zero-length cross-linked peptides.

Main Methods:

  • Utilizes "zero-length" cross-linking reagents that lack spacer arms.
  • Employs multiple cycles of liquid chromatography-tandem mass spectrometry (LC-MS/MS).
  • Features specialized software optimized for zero-length cross-linked peptide identification.

Main Results:

  • Zero-length cross-linking provides highly accurate distance constraints.
  • Developed protocols minimize challenges in identifying cross-linked peptides.
  • Representative data demonstrate the effectiveness of the current protocol.

Conclusions:

  • Advances in zero-length cross-linking enhance structural MS capabilities.
  • Improved identification strategies facilitate the study of protein interactions.
  • This approach offers precise distance information for molecular modeling and validation.