title: 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.
abstract: 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).
authors.affiliation: Kazan Federal University, 18 Kremlevskaya St., Kazan, 420008, Russian Federation, k.usachev@kpfu.ru.
authors.forename: Konstantin S
authors.initials: KS
authors.lastname: Usachev
authors.forename: Andrey V
authors.initials: AV
authors.lastname: Filippov
authors.forename: Oleg N
authors.initials: ON
authors.lastname: Antzutkin
authors.forename: Vladimir V
authors.initials: VV
authors.lastname: Klochkov
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D012996:Solutions
chemical_list: D016229:Amyloid beta-Peptides; D008823:Micelles; D010446:Peptide Fragments; D012996:Solutions; C407125:amyloid beta-protein (10-35); D012967:Sodium Dodecyl Sulfate
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