ArticleJournal of the American Chemical Society2016
Observation of α-Helical Hydrogen-Bond Cooperativity in an Intact Protein.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Amide Monomer-Mediated Solubilization Strategy Enables Nonflammable Deep Eutectic Gel Polymer Electrolytes for High-Temperature-Stable Lithium Metal Batteries.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Measurement of protein non-covalent interactions in buffer and cells.Magnetic resonance letters · 2025Article
- Detecting the Hydrogen Bond Cooperativity in a Protein β-Sheet by H/D Exchange.International journal of molecular sciences · 2022Article
- Anticooperativity of Multiple Halogen Bonds and Its Effect on Stoichiometry of Cocrystals of Perfluorinated Iodobenzenes.Crystal growth & design · 2022Article
- Halogen bonding organocatalysis enhanced through intramolecular hydrogen bonds.Chemical communications (Cambridge, England) · 2022Article
- Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function.Communications biology · 2020Article
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
- Strong Short-Range Cooperativity in Hydrogen-Bond Chains.Angewandte Chemie (International ed. in English) · 2017Article
- Evidences for Cooperative Resonance-Assisted Hydrogen Bonds in Protein Secondary Structure Analogs.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The presence and extent of hydrogen-bonding (H-bonding) cooperativity in proteins remains a fundamental question, which in the past has been studied extensively, mostly by infrared and fluorescence measurements on model peptides. We demonstrate that such cooperativity can be studied in an intact protein by hydrogen/deuterium exchange NMR spectroscopy. The method is based on the fact that substitution of NH by ND in a backbone amide group slightly weakens the N-H···O═C hydrogen bond. Our results show that such substitution at position i in an α-helix impacts the (1)H and (15)N chemical shifts of the amide sites of residues i - 3 to i + 3. Quantum mechanical calculations indicate that the upfield shifts of (1)H and (15)N resonances at site i, observed upon H/D exchanges at sites i - 3, i + 1, i + 2, and i + 3, correspond to a decrease of the ith backbone amide electric dipole moment, which weakens its H-bonding and long-range electrostatic interactions with other backbone amides in the α-helix. These results provide new quantitative insights into the cooperativity of H-bonding in protein α-helices.
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