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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
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Usachev, Konstantin S., Filippov, Andrey V., Antzutkin, Oleg N. and Klochkov, Vladimir V. (2013) 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. European Biophysics Journal, Volume 42 (Number 11-12). pp. 803-810. doi:10.1007/s00249-013-0928-7 ISSN 0175-7571.
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Official URL: http://dx.doi.org/10.1007/s00249-013-0928-7
Abstract
The spatial structure of Alzheimer's amyloid A beta(10-35)-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 A beta(10-35)-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of A beta(10-35)-NH2 were observed. By use of experimental data, the structure of "peptide-micelle" complex was determined; it was found that A beta(10-35)-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35).
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Physics | ||||
Journal or Publication Title: | European Biophysics Journal | ||||
Publisher: | Springer | ||||
ISSN: | 0175-7571 | ||||
Official Date: | December 2013 | ||||
Dates: |
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Volume: | Volume 42 | ||||
Number: | Number 11-12 | ||||
Page Range: | pp. 803-810 | ||||
DOI: | 10.1007/s00249-013-0928-7 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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