Electrostatic potential maps

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! scope="colgroup" colspan="3" | Protein is in the same orientation in all images.
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! scope="colgroup" colspan="3" | Protein [[1pgb]] is in the same orientation in all images.
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|style="width: 250;" width="250"| [[Image:1pgb-EPM-PyMOL.png|200 px]]
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|style="width: 250;" width="250"| [[Image:1pgb-EPM-PyMOL.png|250 px]]
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|style="width: 250;" width="250"| [[Image:1pgb-EPM-iCn3D.png|200 px]]
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|style="width: 250;" width="250"| [[Image:1pgb-EPM-iCn3D.png|250 px]]
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|style="width: 250;" width="250"| [[Image:1pgb-EPM-PyMOL.png|200 px]]
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|style="width: 250;" width="250"| [[Image:1pgb-EPM-PyMOL.png|250 px]]
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| Electrostatic potential map of protein [[1pgb]] rendered by [[PyMOL]].
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| Electrostatic potential map rendered by [[PyMOL]].
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| image2
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| Electrostatic potential map rendered by [[iCn3D]].
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| yyy
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| Van der Waals model colored by charge wtih [[FirstGlance in Jmol]].
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Revision as of 17:40, 25 August 2024

It is revealing to visualize the distribution of electrostatic charges, electrostatic potential, on molecular surfaces. Most protein-protein and protein-ligand interactions are largely electrostatic in nature, via hydrogen bonds and ionic interactions. Their strengths are modulated by the nature of the solvent: pure water or high ionic strength aqueous solution.

Gallery

Protein 1pgb is in the same orientation in all images.
Electrostatic potential map rendered by PyMOL. Electrostatic potential map rendered by iCn3D. Van der Waals model colored by charge wtih FirstGlance in Jmol.
Electrostatic potential map of 1tsj made with the Embedded Python Molecular Viewer from the Center for Computational Structural Biology of the Scripps Research Institute.

Click on the image to enlarge. |}

See Also

References

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz

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