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Distinct Conformational States of the Alzheimer β‐Amyloid Peptide Can Be Detected by High‐Pressure NMR Spectroscopy
Author(s) -
Munte Claudia Elisabeth,
Beck Erlach Markus,
Kremer Werner,
Koehler Joerg,
Kalbitzer Hans Robert
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201301537
Subject(s) - nuclear magnetic resonance spectroscopy , chemistry , spectroscopy , peptide , amyloid (mycology) , nuclear magnetic resonance , stereochemistry , biochemistry , physics , inorganic chemistry , quantum mechanics
Folding under pressure : High‐pressure NMR spectroscopy detects three different conformational states of the Aβ‐peptide in solution: a compactly folded state 1 , a partially folded state 2′ , and a random‐coil like state 2′′ (see plot, p=population). At ambient pressure the folded state 1 dominates which probably has a high affinity to fibrils and thus may promote fibril formation.