ArticleNature structural & molecular biology2022
True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 53 citations in OpenAlex.
- Molecular mechanism of calcium inhibition in viral channelrhodopsins.Nature communications · 2026Article
- Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide.Nature communications · 2025Article
- Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states.Nature structural & molecular biology · 2025Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Flexibility and Hydration of the QJournal of chemical information and modeling · 2025Article
- Engineering of soluble bacteriorhodopsin.Chemical science · 2025Article
- Macromolecular crystallography and biology at the Linac Coherent Light Source.Journal of synchrotron radiation · 2025Article
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.Nature communications · 2025Article
- A DFTB study on the electronic response of encapsulated DNA nucleobases onto chiral CNTs as a sequencer.Scientific reports · 2024Article
- A subgroup of light-driven sodium pumps with an additional Schiff base counterion.Nature communications · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- Crystallographic insights into lipid-membrane protein interactions in microbial rhodopsins.Frontiers in molecular biosciences · 2024Article
- The TR-icOS setup at the ESRF: time-resolved microsecond UV-Vis absorption spectroscopy on protein crystals.Acta crystallographica. Section D, Structural biology · 2024Article
- A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins.The journal of physical chemistry. B · 2023Article
- Mechanisms of inward transmembrane proton translocation.Nature structural & molecular biology · 2023Article
- The Realm of Unconventional Noncovalent Interactions in Proteins: Their Significance in Structure and Function.ACS omega · 2023Review
- Hybrid Quantum Mechanical/Molecular Mechanical Methods For Studying Energy Transduction in Biomolecular Machines.Annual review of biophysics · 2023Review
- Detailed analysis of distorted retinal and its interaction with surrounding residues in the K intermediate of bacteriorhodopsin.Communications biology · 2023Article
- Contribution of the Collective Excitations to the Coupled Proton and Energy Transport along Mitochondrial Cristae Membrane in Oxidative Phosphorylation System.Entropy (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
19 authors at 9 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogen bonds are fundamental to the structure and function of biological macromolecules and have been explored in detail. The chains of hydrogen bonds (CHBs) and low-barrier hydrogen bonds (LBHBs) were proposed to play essential roles in enzyme catalysis and proton transport. However, high-resolution structural data from CHBs and LBHBs is limited. The challenge is that their 'visualization' requires ultrahigh-resolution structures of the ground and functionally important intermediate states to identify proton translocation events and perform their structural assignment. Our true-atomic-resolution structures of the light-driven proton pump bacteriorhodopsin, a model in studies of proton transport, show that CHBs and LBHBs not only serve as proton pathways, but also are indispensable for long-range communications, signaling and proton storage in proteins. The complete picture of CHBs and LBHBs discloses their multifunctional roles in providing protein functions and presents a consistent picture of proton transport and storage resolving long-standing debates and controversies.
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