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Oxidative refolding of amyloidogenic variants of human lysozyme.

Abstract:

The oxidative refolding of human lysozyme and its two best characterised amyloidogenic variants, Ile56Thr and Asp67His, has been investigated in vitro by means of the concerted application of a range of biophysical techniques. The results show that in each case the ensemble of reduced denatured conformers initially collapses into a large number of unstructured intermediates with one or two disulphide bonds, the majority of which then fold to form the native-like three-disulphide intermediate,...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2005.06.035

Authors


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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Journal of molecular biology
Volume:
351
Issue:
3
Pages:
662-671
Publication date:
2005-08-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:06229ea6-3bdf-4fbd-9868-f25aa76de87b
Source identifiers:
33171
Local pid:
pubs:33171

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