title: The cleavage domain of the amyloid precursor protein transmembrane helix does not exhibit above-average backbone dynamics.
abstract: Wobbly backbone: The backbone dynamics of the amyloid precursor protein (APP) transmembrane helix was compared to those of other transmembrane domains. In contrast to expectation, no above-average backbone dynamics was found for the APP transmembrane helix; the dynamics thus appears not to be optimized for cleavage.
authors.affiliation: Lehrstuhl Chemie der Biopolymere, Technische Universität München and Munich Center For Integrated Protein Science (CIPSM), Weihenstephaner Berg 3, 85354 Freising (Germany); Current address: Roche Diagnostics GmbH, Nonnenwald 2, 82377 Penzberg (Germany).
authors.forename: Oxana
authors.initials: O
authors.lastname: Pester
authors.forename: Alexander
authors.initials: A
authors.lastname: Götz
authors.forename: Gerd
authors.initials: G
authors.lastname: Multhaup
authors.forename: Christina
authors.initials: C
authors.lastname: Scharnagl
authors.forename: Dieter
authors.initials: D
authors.lastname: Langosch
mesh_terms: D016564:Amyloid beta-Protein Precursor / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D059748:Proteolysis
chemical_list: D016564:Amyloid beta-Protein Precursor; D010446:Peptide Fragments
keywords: Alzheimer's disease; amide exchange; amyloid precursor proteins; membrane proteins; molecular dynamics; transmembrane domains