ArticleScience advances2022
Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Predicting Iron-Sulfur Cluster Redox Potentials: A Simple Model Derived from Protein Structures.ACS omega · 2025Article
- "Seeing Is Believing": How Neutron Crystallography Informs Enzyme Mechanisms by Visualizing Unique Water Species.Biology · 2024Review
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
- Site-specific relaxation of peptide bond planarity induced by electrically attracted proton/deuteron observed by neutron crystallography.Protein science : a publication of the Protein Society · 2023Article
- Description of peptide bond planarity from high-resolution neutron crystallography.Biophysics and physicobiology · 2023Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The planarity of the peptide bond is important for the stability and structure formation of proteins. However, substantial distortion of peptide bonds has been reported in several high-resolution structures and computational analyses. To investigate the peptide bond planarity, including hydrogen atoms, we report a 1.2-Å resolution neutron structure of the oxidized form of high-potential iron-sulfur protein. This high-resolution neutron structure shows that the nucleus positions of the amide protons deviate from the peptide plane and shift toward the acceptors. The planarity of the H─N─C═O plane depends strongly on the pyramidalization of the nitrogen atom. Moreover, the orientation of the amide proton of Cys
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Registered trials
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