Distinct conformational states of the alzheimer β-amyloid peptide can be detected by high-pressure NMR spectroscopy

Angewandte Chemie - International Edition

Volumn 52, Issue 34, 2013, Pages 8943-8947

  Munte, Claudia Elisabeth ^a,b   Beck Erlach, Markus ^a   Kremer, Werner ^a   Koehler, Joerg ^a   Kalbitzer, Hans Robert ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Alzheimer's disease; amyloid peptides; high pressure chemistry; NMR spectroscopy

Indexed keywords

ALZHEIMER'S DISEASE; AMBIENT PRESSURES; AMYLOID PEPTIDES; CONFORMATIONAL STATE; FIBRIL FORMATION; HIGH AFFINITY; HIGH-PRESSURE CHEMISTRY; HIGH-PRESSURE NMR;

GLYCOPROTEINS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

CONFORMATIONS;

AMYLOID BETA PROTEIN;

ALZHEIMER DISEASE; AMYLOID Β-PEPTIDES; ARTICLE; HIGH-PRESSURE CHEMISTRY; HUMAN; IMMUNOLOGY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PATHOLOGY;

ALZHEIMER'S DISEASE; AMYLOID Β-PEPTIDES; HIGH-PRESSURE CHEMISTRY; NMR SPECTROSCOPY;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY;

EID: 84882253108     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201301537     Document Type: Article

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