Title : Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes It Soluble.

Pub. Date : 2015 Dec 11

PMID : 26487720






2 Functional Relationships(s)
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1 Surprisingly, two-dimensional solid state NMR shows that the contact between Phe(19) and Leu(34) residues, observed in full-length Abeta and Abeta18-35, is still intact in these fibrils. Leucine amyloid beta precursor protein Homo sapiens
2 We conclude that the self-assembly of Abeta is critically dependent on the hairpin turn and on the contact between the Phe(19) and Leu(34) regions, making them potentially sensitive targets for Alzheimer"s therapeutics. Leucine amyloid beta precursor protein Homo sapiens