mriselMagnetic Resonance in SolidsMagnetic Resonance in Solids2072-5981Kazan Federal Universitymrisel-156Research ArticleСтатьиSpatial structure of tetrapeptide N-AC-Ser-Phe-Val-Gly-OMe in "protein-micelle of sodium dodecyl sulfate" complex and in solid state by NMR spectroscopyBlokhinD. S.

Kremlevskaya, 18, Kazan 420008

BergerS.

Augustusplatz 10, 04109 Leipzig

KlochkovV. V.

Kremlevskaya, 18, Kazan 420008

vklochko@kpfu.ruKazan Federal UniversityRussian FederationUniversity of LeipzigGermany20131901202415213202 (7 pp.)Copyright © Blokhin D.S., Berger S., Klochkov V.V., 20242024Blokhin D.S., Berger S., Klochkov V.V.Blokhin D.S., Berger S., Klochkov V.V.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.mrsej.ru/jour/article/view/156

In the present paper the applicability of a structure determination for a four amino acid residues containing oligopeptide N-Ac-Ser-Phe-Val-Gly-OMe was investigated. The spatial structure of the "tetrapeptide (N-Ac-Ser-Phe-Val-Gly-OMe) - sodium dodecyl sulfate micelle" complex in aqueous solution was studied by 2D nuclear magnetic resonance (NMR) spectroscopy. The complexation was confirmed NOEs signs and values in the presence of sodium dodecyl sulfate. The spatial structure of the tetrapeptide in the complex was determined by 2D NOESY NMR spectroscopy. In present paper by the comparison 13C NMR chemical shifts was shown that tetra peptide's spatial structure in solid state and tetrapeptide structure in "peptide-micelle" complex are identical.

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The authors declare that there are no conflicts of interest present.