Аннотации:
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 Aβ 10-35-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of Ab10-35-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).© European Biophysical Societies' Association 2013.