Journal article icon

Journal article

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,...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1016/j.jmb.2005.06.035

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
Journal:
Journal of molecular biology
Volume:
351
Issue:
3
Pages:
662-671
Publication date:
2005-08-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:33171
UUID:
uuid:06229ea6-3bdf-4fbd-9868-f25aa76de87b
Local pid:
pubs:33171
Source identifiers:
33171
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP