Structural heterogeneity in transmembrane amyloid precursor protein Homodimer is a consequence of environmental selection

Journal of the American Chemical Society

Volumn 136, Issue 27, 2014, Pages 9619-9626

  Dominguez, Laura ^a   Foster, Leigh ^a   Meredith, Stephen C ^b   Straub, John E ^a   Thirumalai, D ^c  

^a Boston University   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

^c Bldg 142   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; MICELLES; PROTEINS;

ALZHEIMERS DISEASE; AMYLOID PRECURSOR PROTEINS; C-TERMINAL FRAGMENTS; COARSE GRAINED MODELS; MULTI-SCALE APPROACHES; STRUCTURAL HETEROGENEITY; STRUCTURAL STUDIES; SURFACTANT MICELLES;

GLYCOPROTEINS;

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; HOMODIMER; SURFACTANT; MICELLE;

ALZHEIMER DISEASE; ARTICLE; ATOM; BILAYER MEMBRANE; CONCEPTUAL FRAMEWORK; DIMERIZATION; ENERGY; ENVIRONMENTAL FACTOR; MICELLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; SIMULATION; CHEMICAL STRUCTURE; CHEMISTRY;

AMYLOID BETA-PROTEIN PRECURSOR; MICELLES; MODELS, MOLECULAR; PROTEIN CONFORMATION;

EID: 84903973868     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja503150x     Document Type: Article

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