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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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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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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Membrane Fluidity01:26

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
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Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and

Hugh R Higinbotham1,2, Christine A Arbour2,3, Barbara Imperiali2,3

  • 1Department of Physics, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.

Protein Science : a Publication of the Protein Society
|October 24, 2025
PubMed
Summary

We developed a new method combining structural bioinformatics, molecular simulation, and single-molecule Förster Resonance Energy Transfer (FRET) microscopy to study membrane protein dynamics. This approach reveals how small monotopic phosphoglycosyl transferases change shape upon ligand binding, crucial for glycoconjugate biosynthesis.

Keywords:
glycoconjugate biosynthesismembrane proteinmolecular dynamicsnon‐canonical amino acid mutagenesissingle‐molecule FRETsubstrate specificity

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Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Integral membrane proteins play vital roles in cellular processes.
  • Understanding their conformational dynamics is key to elucidating function.
  • The small monotopic phosphoglycosyl transferase (SmPGT) superfamily is essential for glycoconjugate biosynthesis in prokaryotes.

Purpose of the Study:

  • To develop and apply an integrated strategy for observing ligand-dependent conformational dynamics of integral membrane proteins in situ.
  • To investigate the structure-function relationship within the SmPGT superfamily.
  • To validate the role of protein motion in ligand binding for PglC.

Main Methods:

  • Integrated approach using structural bioinformatics, molecular simulation, and single-molecule Förster Resonance Energy Transfer (FRET) microscopy.
  • Development of a platform for monitoring intramolecular protein dynamics in a native-like lipid environment using styrene-maleic acid liponanoparticles (SMALPs).
  • Utilized selective cysteine protein labeling, non-canonical amino acid mutagenesis, and click chemistry to create dual-labeled PglC variants.

Main Results:

  • Identified substrate-specific structural features across the SmPGT superfamily.
  • Correlated ligand-dependent conformational dynamics with structural features using all-atom simulations.
  • Demonstrated that conformational changes of PglC upon inhibitor binding correlate with inhibitor potency.

Conclusions:

  • The developed single-molecule FRET-SMALP strategy effectively monitors protein dynamics in a native-like membrane environment.
  • This approach is adaptable for studying diverse SmPGTs with varying substrate specificities.
  • Structure prediction and molecular dynamics support significant conformational changes upon ligand binding in this protein superfamily.