z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom