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NMR Studies of the Mn2+ Interactions with Amyloid Peptide A beta 13-23 in Water Environmentстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 11 мая 2022 г.
- Авторы: Abdrakhmanov Rustam, Blokhin Dmitriy, Usachev Konstantin, Karataeva Farida, Klochkov Vladimir
- Журнал: BioNanoScience
- Том: 7
- Номер: 1
- Год издания: 2017
- Первая страница: 204
- Последняя страница: 206
- DOI: 10.1007/s12668-016-0317-7
- Аннотация: In this paper, binding of Mn2+ ions to the fragment of beta-amyloid peptide (A beta(13-23)) was studied. Manganese complexation induces important structural changes within the C-terminal segment of the peptide. Investigation of peptide-metal ion binding was made by MnCl2 salt titration and recording 2D H-1-H-1 NMR TOCSY spectra (TOtal Correlation SpectroscopY). Multidimensional NMR techniques were performed to understand the details of the conformational behavior of the peptide and to reveal the metal-binding sites. According to changes in NMR spectra, the manganese-binding center of the A beta(13-23) peptide is associated with the aspartate residue
- Добавил в систему: Усачев Константин Сергеевич