ArticleNature chemical biology2016
A prevalent intraresidue hydrogen bond stabilizes proteins.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- α-Alkylated α-amino acids reduce the aggregation of unfolded peptides.RSC advances · 2026Article
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- Thioamides in C5 Hydrogen Bonds: Implications for Protein β-Strands.The Journal of organic chemistry · 2025Article
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- Molecular Insights into α-Synuclein Fibrillation: A Raman Spectroscopy and Machine Learning Approach.ACS chemical neuroscience · 2025Article
- α-Methylation Enables the X-ray Crystallographic Observation of Oligomeric Assemblies Formed by a β-Hairpin Peptide Derived from Aβ.The Journal of organic chemistry · 2025Article
- Nucleic-acid-base photofunctional cocrystal for information security and antimicrobial applications.Nature communications · 2024Article
- Synthesis, derivatization, and conformational scanning of peptides containing N-Aminoglycine.Methods in enzymology · 2024Article
- Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method.PNAS nexus · 2023Article
- Raman Fingerprints of SARS-CoV-2 Omicron Subvariants: Molecular Roots of Virological Characteristics and Evolutionary Directions.ACS infectious diseases · 2023Article
- Effects of chirality and side chain length in COrganic & biomolecular chemistry · 2023Article
- Quantifying Amide-Aromatic Interactions at Molecular and Atomic Levels: Experimentally-determined Enthalpic and Entropic Contributions to Interactions of Amide spbioRxiv : the preprint server for biology · 2023Article
- The "Beacon" Structural Model of Protein Folding: Application for Trp-Cage in Water.Molecules (Basel, Switzerland) · 2023Article
- Length-Dependent Transition from Extended to Folded Shapes in Short Oligomers of an Azetidine-Based α-Amino Acid: The Critical Role of NH···N H-Bonds.Molecules (Basel, Switzerland) · 2023Article
- The Realm of Unconventional Noncovalent Interactions in Proteins: Their Significance in Structure and Function.ACS omega · 2023Review
- Disassembly of Amyloid Fibril with Infrared Free Electron Laser.International journal of molecular sciences · 2023Review
- Detecting the Hydrogen Bond Cooperativity in a Protein β-Sheet by H/D Exchange.International journal of molecular sciences · 2022Article
- SM-COLSARSPROT: Highly Immunogenic Supramutational Synthetic Peptides Covering the World's Population.Frontiers in immunology · 2022Article
- Bispidine as a β-strand nucleator: from a β-arch to self-assembled cages and vesicles.Chemical science · 2021Article
- N-H⋯X interactions stabilize intra-residue C5 hydrogen bonded conformations in heterocyclic α-amino acid derivatives.Chemical science · 2021Article
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2 authors.
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Abstract
Current limitations in de novo protein structure prediction and design suggest an incomplete understanding of the interactions that govern protein folding. Here we demonstrate that previously unappreciated hydrogen bonds occur within proteins between the amide proton and carbonyl oxygen of the same residue. Quantum calculations, infrared spectroscopy, and nuclear magnetic resonance spectroscopy show that these interactions share hallmark features of canonical hydrogen bonds. Biophysical analyses demonstrate that selective attenuation or enhancement of these C5 hydrogen bonds affects the stability of synthetic β-sheets. These interactions are common, affecting approximately 5% of all residues and 94% of proteins, and their cumulative impact provides several kilocalories per mole of conformational stability to a typical protein. C5 hydrogen bonds especially stabilize the flat β-sheets of the amyloid state, which is linked with Alzheimer's disease and other neurodegenerative disorders. Inclusion of these interactions in computational force fields would improve models of protein folding, function, and dysfunction.
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