Familial Alzheimer’s disease mutations alter the stability of the amyloid -protein monomer folding nucleus
نویسندگان
چکیده
*Division of Molecular and Vascular Medicine, Beth Israel Deaconess Medical Center, and Department of Medicine, Harvard Medical School, Boston, MA 02215; †Gustaf A. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610; ‡Department of Physics, Massachusetts Institute of Technology, Cambridge, MA 02139; and §Department of Neurology, David Geffen School of Medicine, and Molecular Biology Institute and Brain Research Institute, University of California, Los Angeles, CA 90095
منابع مشابه
Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus.
Amyloid beta-protein (Abeta) oligomers may be the proximate neurotoxins in Alzheimer's disease (AD). Recently, to elucidate the oligomerization pathway, we studied Abeta monomer folding and identified a decapeptide segment of Abeta, (21)Ala-(22)Glu-(23)Asp-(24)Val-(25)Gly-(26)Ser-(27)Asn-(28)Lys-(29)Gly-(30)Ala, within which turn formation appears to nucleate monomer folding. The turn is stabil...
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