Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment

Article ID	Journal	Published Year	Pages	File Type
10871398	FEBS Letters	2012	6 Pages	PDF

Abstract

âº We determined the left-handed dimeric structure of transmembrane domain of amyloid precursor protein. âº The dimerization mechanism of APP is important for understanding the molecular mechanism of production of amyloid-Î² peptide. âº Familial mutations of amyloid precursor protein can affect its lateral dimerization.

Keywords

Aβ HSQC APP DPC NOESY NOE amyloid β-peptide nuclear overhauser effect Dimerization Alzheimer’s disease Juxtamembrane transmembrane domain Dodecylphosphocholine Spatial structure NOE spectroscopy NMR spectroscopy transmembrane heteronuclear single-quantum correlation amyloid precursor protein