Form of presentation | Articles in international journals and collections |
Year of publication | 2016 |
|
Karataeva Farida Khaydarovna, author
Klochkov Vladimir Vasilevich, author
Usachev Konstantin Sergeevich, author
|
|
Abdrakhmanov Rustam Zhamilevich, postgraduate kfu
|
Bibliographic description in the original language |
Binding of Mn2+ ions to the fragment of beta-amyloid peptide (Aβ13-23) was studied. Manganese complexation induces important structural changes within the C-terminal segment of the peptide. Investigation of peptide Ab metal ion binding was made by MnCl2 salt titration and recording 2D 1H-1H 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 metalbinding sites. According to changes in NMR spectra, the manganese-binding center of the Aβ13-23 peptide is associated with the aspartate residue. |
Keywords |
Amyloid peptide Aβ13-23, NMR spectroscopy,
Mn2+ ions |
The name of the journal |
BioNanoScience
|
Please use this ID to quote from or refer to the card |
https://repository.kpfu.ru/eng/?p_id=148699&p_lang=2 |
Full metadata record |
Field DC |
Value |
Language |
dc.contributor.author |
Karataeva Farida Khaydarovna |
ru_RU |
dc.contributor.author |
Klochkov Vladimir Vasilevich |
ru_RU |
dc.contributor.author |
Usachev Konstantin Sergeevich |
ru_RU |
dc.contributor.author |
Abdrakhmanov Rustam Zhamilevich |
ru_RU |
dc.date.accessioned |
2016-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2016-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2016 |
ru_RU |
dc.identifier.citation |
Binding of Mn2+ ions to the fragment of beta-amyloid peptide (Aβ13-23) was studied. Manganese complexation induces important structural changes within the C-terminal segment of the peptide. Investigation of peptide Ab metal ion binding was made by MnCl2 salt titration and recording 2D 1H-1H 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 metalbinding sites. According to changes in NMR spectra, the manganese-binding center of the Aβ13-23 peptide is associated with the aspartate residue. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/eng/?p_id=148699&p_lang=2 |
ru_RU |
dc.description.abstract |
BioNanoScience |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Amyloid peptide Aβ13-23 |
ru_RU |
dc.subject |
NMR spectroscopy |
ru_RU |
dc.subject |
Mn2+ ions |
ru_RU |
dc.title |
NMR Studies of the Mn2+ Interactions with Amyloid Peptide
Aβ13-23 in Water Environment |
ru_RU |
dc.type |
Articles in international journals and collections |
ru_RU |
|