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• W2265551517 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 1H and 15N chemical shifts of the amide sites of residues i – 3 to i + 3. Quantum mechanical calculations indicate that the upfield shifts of 1H and 15N 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." @default.
• W2265551517 created "2016-06-24" @default.
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• W2265551517 date "2016-02-08" @default.
• W2265551517 modified "2023-10-16" @default.
• W2265551517 title "Observation of α-Helical Hydrogen-Bond Cooperativity in an Intact Protein" @default.
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• W2265551517 doi "https://doi.org/10.1021/jacs.5b13140" @default.
• W2265551517 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5575832" @default.
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• W2265551517 hasPublicationYear "2016" @default.
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