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Journal article

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.

Abstract:

Hydrogen exchange experiments monitored by NMR and mass spectrometry reveal that the amyloidogenic D67H mutation in human lysozyme significantly reduces the stability of the beta-domain and the adjacent C-helix in the native structure. In addition, mass spectrometric data reveal that transient unfolding of these regions occurs with a high degree of cooperativity. This behavior results in the occasional population of a partially structured intermediate in which the three alpha-helices that for...

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Publication status:
Published

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Publisher copy:
10.1038/nsb768

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Journal:
Nature structural biology
Volume:
9
Issue:
4
Pages:
308-315
Publication date:
2002-04-05
DOI:
ISSN:
1072-8368
URN:
uuid:c4a7f24d-b6c9-453b-b105-e9df3a2e76d2
Source identifiers:
59239
Local pid:
pubs:59239

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