Title : Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy.

Pub. Date : 2011 Mar 16

PMID : 21341665






2 Functional Relationships(s)
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Protein Name
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1 Selective quenching observed in (13)C SSNMR of Cu(2+)-bound Abeta(1-40) suggested that primary Cu(2+) binding sites in Abeta(1-40) fibrils include N(epsilon) in His-13 and His-14 and carboxyl groups in Val-40 as well as in Glu sidechains (Glu-3, Glu-11, and/or Glu-22). Histidine amyloid beta precursor protein Homo sapiens
2 Selective quenching observed in (13)C SSNMR of Cu(2+)-bound Abeta(1-40) suggested that primary Cu(2+) binding sites in Abeta(1-40) fibrils include N(epsilon) in His-13 and His-14 and carboxyl groups in Val-40 as well as in Glu sidechains (Glu-3, Glu-11, and/or Glu-22). Histidine amyloid beta precursor protein Homo sapiens