Solid State NMR study on the Dimer Structure of the Transmembrane Region of Amyloid Precursor Protein

摘要

Abstract Solid-state NMR spectroscopy is used to establish the structural features of the transmembrane (TM) domain of amyloid precursor protein (APP) which facilitate proteolysis. Using synthetic peptides, we show that the TM domain forms an a-helical homodimer mediated by consecutive GxxxG motifs.