- 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,...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.jmb.2005.06.035
-
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- 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
- Copyright date:
- 2005
Journal article
Oxidative refolding of amyloidogenic variants of human lysozyme.
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