[NMR paper] Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid A?10-35 peptide in solution and in SDS micelles.

[nmrlearner]

Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid A?10-35 peptide in solution and in SDS micelles.

Related Articles Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid A?10-35 peptide in solution and in SDS micelles.

Eur Biophys J. 2013 Dec;42(11-12):803-10

Authors: Usachev KS, Filippov AV, Antzutkin ON, Klochkov VV

Abstract
The spatial structure of Alzheimer's amyloid A?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?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?10-35-NH2 were observed. By use of experimental data, the structure of "peptide-micelle" complex was determined; it was found that A?10-35-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35).


PMID: 24037178 [PubMed - indexed for MEDLINE]



More...