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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

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

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

Decoding Protein Dynamics in Cells Using Chemical Cross-Linking and Hierarchical Analysis.

Beirong Zhang^1,2, Zhou Gong³, Lili Zhao^1,2

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

Summary

This summary is machine-generated.

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:

Alphafold2 In Vivo Cross-Linking Mass Spectrometry Protein Dynamics Protein 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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Published on: March 9, 2010

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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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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

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.