ArticleProtein science : a publication of the Protein Society2017
Effects of aligned α-helix peptide dipoles on experimental electrostatic potentials.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Multifaceted aspects of charge transfer.Physical chemistry chemical physics : PCCP · 2020Article
- Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Determination of chemical identity and occupancy from experimental density maps.Protein science : a publication of the Protein Society · 2018Article
- On the relationship between cumulative correlation coefficients and the quality of crystallographic data sets.Protein science : a publication of the Protein Society · 2017Article
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3 authors.
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Abstract
Aligned protein α-helix dipoles have been implicated in protein function and structure. The recent breakthroughs in high-resolution electron microscopy (EM) of macromolecules makes it possible to explore fundamental aspects of structural biology at the detailed molecular level. The electrostatic potential (ESP) generated by aligned protein α-helix dipole should be observable in high-resolution EM maps despite the fact that the effect may be partially screened by induced electric fields. Here, we show that aligned backbone dipoles in protein α-helices account for long-range features in the protein ESP functions. Our results are consistent with experimental EM maps and density functional theory calculations, including direct Fourier summation for proper calculation of the ESP due to the nonlocal nature of the ESP function from aligned dipoles and other partial atomic charges.
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