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

dc.creatorMunte, Claudia Elisabeth
dc.creatorErlach, Markus Beck
dc.creatorKremer, Werner
dc.creatorKalbitzer, Hans Robert
dc.creatorKoehler, Joerg
dc.date.accessioned2014-06-02T16:53:37Z
dc.date.accessioned2018-07-04T16:46:08Z
dc.date.available2014-06-02T16:53:37Z
dc.date.available2018-07-04T16:46:08Z
dc.date.created2014-06-02T16:53:37Z
dc.date.issued2013-08
dc.identifierAngewandte Chemie International Edition, Weinheim : Wiley-VCH Verlag, v. 52, n. 34, p. 8943-8947, Aug. 2013
dc.identifier1433-7851
dc.identifierhttp://www.producao.usp.br/handle/BDPI/45195
dc.identifier10.1002/anie.201301537
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1640108
dc.description.abstractFolding 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.
dc.languageeng
dc.publisherWiley-VCH Verlag
dc.publisherWeinheim
dc.relationAngewandte Chemie International Edition
dc.rightsCopyright WILEY-VCH Verlag GmbH & Co. KGaA
dc.rightsrestrictedAccess
dc.subjectAlzheimer’s disease
dc.subjectAmyloid β-peptides
dc.subjectHigh-pressure chemistry
dc.subjectNMR spectroscopy
dc.titleDistinct conformational states of the Alzheimer β-amyloid peptide can be detected by high-pressure NMR spectroscopy
dc.typeArtículos de revistas


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