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Updated: May 18, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Spatial structure of heptapeptide Aβ(16-22) (beta-amyloid Aβ(1-40) active fragment) in solution and in complex with
Konstantin S Usachev1, Sergej V Efimov, Ajdar R Yulmetov
1Kazan (Volga Region) Federal University, 18 Kremlevskaya St., 420008, Kazan, Russian Federation.
Abstract:
The spatial structure of an active fragment of beta-amyloid Aβ(1-40) heptapeptide Aβ(16-22) (Lys-Leu-Val-Phe-Phe-Ala-Glu) in aqueous buffer solution and in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by (1)H NMR spectroscopy and two-dimensional NMR (TOCSY, HSQC-HECADE (Heteronuclear Couplings from ASSCI-domain experiments with E.COSY-type crosspeaks), NOESY) spectroscopy. Complex formation was confirmed by the chemical shift changes of the heptapeptide's (1)H NMR spectra, as well as by the signs and values of the NOE effects in different environments. We compared the spatial structure of the heptapeptide in borate buffer solution and in complex with a model of the cell surface membrane.
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