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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.2K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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Related Experiment Video

Updated: Jul 24, 2025

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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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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Decoding Protein Dynamics in Cells Using Chemical Cross-Linking and Hierarchical Analysis.

Beirong Zhang1,2, Zhou Gong3, Lili Zhao1,2

  • 1CAS Key Labratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian, 116023, China.

Angewandte Chemie (International Ed. in English)
|July 5, 2023
PubMed
Summary

We developed a new method to study protein dynamics in cells using chemical cross-linking and computational analysis. This approach reveals detailed protein structures and motions, advancing our understanding of cellular protein functions.

Keywords:
Alphafold2In Vivo Cross-LinkingMass SpectrometryProtein DynamicsProtein Structures

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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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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Protein dynamics are essential for cellular functions.
  • Intracellular environments significantly impact protein dynamics, especially for intrinsically disordered proteins (IDPs).

Purpose of the Study:

  • To introduce a hierarchical decoding strategy for investigating in vivo protein dynamics.
  • To characterize full-length protein structures and dynamic features within cells.

Main Methods:

  • Utilized chemical cross-linking mass spectrometry to capture structural information.
  • Employed computational analysis with distance restraints derived from cross-links.
  • Leveraged AlphaFold2-predicted structures to infer protein dynamics.

Main Results:

  • Successfully characterized the full-length structure of multi-domain proteins, including their dynamic features.
  • Provided a comprehensive description of the intrinsic motion of intrinsically disordered proteins (IDPs).

Conclusions:

  • The proposed hierarchical strategy enhances the understanding of protein dynamics in vivo.
  • This approach offers significant potential for elucidating molecular mechanisms underlying protein functions in cellular environments.