A server and database for dipole moments of proteins
Open accessAbstract
An Internet server at http://bip.weizmann.ac.il/dipol calculates the net charge, dipole moment and mean radius of any 3D protein structure or its constituent peptide chains, and displays the dipole vector superimposed on a ribbon backbone of the protein. The server can also display the angle between the dipole and a selected list of amino acid residues in the protein. When the net charges and dipole moments of approximately 12 000 non-homologous PDB biological units (PISCES set), and their unique chains of length 50 residues or longer, were examined, the great majority of both charges and dipoles fell into a very narrow range of values, with long extended tails containing a few extreme outliers. In general, there is no obvious relation between a protein's charge or dipole moment and its structure or function, so that its electrostatic properties are highly specific to the particular protein, except that the majority of chains with very large positive charges or dipoles bind to ribosomes or interact with nucleic acids.
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The Septin complex dipole moment is approximately five standard deviations higher than the median value of 542.66 D derived from 14,960 protein structures.
“Significantly, this dipole moment is approximately five standard deviations higher than the median value of 542.66 D derived from the analysis of 14,960 protein structures [49].”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [49]
The mitotic Septin complex consisting of Septin 2, 6 and 7 has a calculated dipole moment of 2711 Debyes (D).
“The mitotic Septin complex consisting of Septin 2, 6 and 7, possesses a high calculated dipole moment of 2711 Debyes (D)”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [49]
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Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit
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An Evidence-Based Review of Alternating Electric Fields Therapy for Malignant Gliomas
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- Authors
- Felder, C. E., Prilusky, J., Silman, I., & Sussman, J. L.
- Affiliations
- Weizmann Institute of Science (IL)
- Corresponding author
- Sussman, J. L.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-05-08
- Volume
- 35
- Issue
- Web Server
- Pages
- W512-W521
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC1933167
- OpenAlex
- W2047608438
- Cited by
- 206
- References
- 21
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 13 · 2023: 14 · 2022: 8 · 2021: 12 · 2020: 14 · 2019: 15 · 2018: 10 · 2017: 9 · 2016: 17 · 2015: 17 · 2014: 5 · 2013: 10 · 2012: 8
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- net charge, protein electrostatics, protein structure database, ribosome binding, nucleic acid binding
- MeSH terms
- Biophysics, Computer Simulation, Enzymes, Fungal Proteins, Mathematics, Models, Molecular, Protein Conformation, Proteins, Software, Models, Statistical, Databases, Bibliographic, Protein Structure, Secondary, Computational Biology, Databases, Protein
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