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• W2042181303 endingPage "12269" @default.
• W2042181303 startingPage "12263" @default.
• W2042181303 abstract "The backbone conformation of peptides and proteins is completely defined by the torsion angles (φ,ψ,ω) of each amino acid residue along the polypeptide chain. We demonstrate a solid-state NMR method based on heteronuclear distance measurements for determining (φ,ψ) angles. Simple and reliable deuterium phase modulated pulses (PM5) reintroduce dipolar couplings between 2H and a spin-1/2 nucleus. Measuring the 13Ci-1{2Hiα} REDOR distance across a peptide bond results in the torsion angle φi as a consequence of the restricted geometry of the peptide backbone. The 15Ni+1{2Hiα} REDOR distance across a peptide bond defines the torsion angle ψi. This approach is demonstrated for both the 3-spin X{2H2}REDOR case of glycine and the 2-spin X{2H}REDOR case, represented by l-alanine, using two different tripeptides. It is shown that the technique can handle multiple sample conformations. PM5-REDOR decay curves of the ψ angle show distinctly different behaviors between α-helix and β-sheet backbone conformations." @default.
• W2042181303 created "2016-06-24" @default.
• W2042181303 creator A5005400349 @default.
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• W2042181303 creator A5053259295 @default.
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• W2042181303 date "2000-11-21" @default.
• W2042181303 modified "2023-09-30" @default.
• W2042181303 title "Solid-State NMR Determination of Peptide Torsion Angles: Applications of ²H-Dephased REDOR" @default.
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• W2042181303 doi "https://doi.org/10.1021/ja000489w" @default.
• W2042181303 hasPublicationYear "2000" @default.
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