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Related Concept Videos

Protein Dynamics in Living Cells01:19

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...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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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Related Experiment Video

Updated: Jul 10, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Two-level approach to efficient visualization of protein dynamics.

Ove Daae Lampe1, Ivan Viola, Nathalie Reuter

  • 1Christian Michelsen Research, Norway. ove.lampe@cmr.no

IEEE Transactions on Visualization and Computer Graphics
|October 31, 2007
PubMed
Summary

We developed a faster visualization method for protein dynamics by rendering residues instead of individual atoms. This approach enhances the understanding of protein structure and function in bioinformatics.

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Related Experiment Videos

Last Updated: Jul 10, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

  • Structural Biology
  • Computational Biology
  • Bioinformatics

Background:

  • Proteins exhibit flexibility, with large-scale movements (slow dynamics) crucial for their function.
  • Visualizing these slow dynamics in large protein assemblies is computationally challenging.

Purpose of the Study:

  • To present a novel two-level rendering approach for visualizing slow dynamics in large protein assemblies.
  • To improve the efficiency and precision of visualizing protein structural changes.

Main Methods:

  • Implemented a hierarchical rendering model based on protein structure.
  • Represented residues as single vertices, updating their position and rotation.
  • Generated atoms on-the-fly using GPU geometry shaders.
  • Utilized billboards instead of tessellated spheres for atom representation.

Main Results:

  • Achieved significantly faster visualization speeds compared to traditional methods.
  • Maintained pixel-precise rendering of protein structures.
  • Demonstrated the approach's effectiveness in a collaborative bioinformatics project.

Conclusions:

  • The two-level rendering approach effectively visualizes slow protein dynamics.
  • This method offers a computationally efficient and precise tool for bioinformatics research.
  • The technique aids in understanding the functional implications of protein flexibility.