Electrostatic potential maps
From Proteopedia
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- | + | |style="width: 210;" width="200"| [[Image:1pgb-EPM-PyMOL.png|200 px]] | |
- | + | |style="width: 210;" width="200"| [[Image:1pgb-EPM-PyMOL.png|200 px]] | |
- | + | |style="width: 210;" width="200"| [[Image:1pgb-EPM-PyMOL.png|200 px]] | |
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+ | | Electrostatic potential map of protein [[1pgb]] rendered by [[PyMOL]]. | ||
+ | | image2 | ||
+ | | yyy | ||
+ | |} | ||
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+ | {| class="wikitable" | ||
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| [[Image:Electrostatic potential 1tsj.PNG|200 px]] || Electrostatic potential map of [[1tsj]] made with the [https://epmv.scripps.edu/ Embedded Python Molecular Viewer] from the [https://ccsb.scripps.edu/ Center for Computational Structural Biology] of the Scripps Research Institute. | | [[Image:Electrostatic potential 1tsj.PNG|200 px]] || Electrostatic potential map of [[1tsj]] made with the [https://epmv.scripps.edu/ Embedded Python Molecular Viewer] from the [https://ccsb.scripps.edu/ Center for Computational Structural Biology] of the Scripps Research Institute. | ||
+ | |} | ||
Click on the image to enlarge. | Click on the image to enlarge. |
Revision as of 17:33, 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
![]() | ![]() | ![]() |
Electrostatic potential map of protein 1pgb rendered by PyMOL. | image2 | yyy |
| 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
- Electrostatic interactions in Proteopedia.
- Jmol/Electrostatic potential methods.
- Isopotential Map in Wikipedia
- Delphi Web Server