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Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid Aβ10-35 peptide in solution and in SDS micelles
Kazan (Volga Region) Federal University, Kazan.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0002-6810-1882
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0003-1067-7990
Kazan (Volga Region) Federal University, Kazan.
2013 (English)In: European Biophysics Journal, ISSN 0175-7571, E-ISSN 1432-1017, Vol. 42, no 11-12, p. 803-810Article in journal (Refereed) Published
Abstract [en]

The spatial structure of Alzheimer's amyloid Aβ10-35-NH2 peptide in aqueous solution at pH 7.3 and in SDS micelles was investigated by use of a combination of the residual dipolar coupling method and two-dimensional NMR spectroscopy (TOCSY, NOESY). At pH 7.3 Aβ10-35-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of Aβ10-35-NH2 were observed. By use of experimental data, the structure of "peptide-micelle" complex was determined; it was found that Aβ10-35-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35). © 2013 European Biophysical Societies' Association.

Place, publisher, year, edition, pages
2013. Vol. 42, no 11-12, p. 803-810
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
Identifiers
URN: urn:nbn:se:ltu:diva-3146DOI: 10.1007/s00249-013-0928-7Local ID: 0eeeee59-4490-474e-9a87-e91912367256OAI: oai:DiVA.org:ltu-3146DiVA: diva2:976002
Note
Validerad; 2013; 20130924 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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