Oxidative refolding of amyloidogenic variants of human lysozyme.

Journal article

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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Role:

Author

Institution:

University of Oxford

Division:

MPLS

Department:

Chemistry

Sub department:

Inorganic Chemistry

Role:

Author

Role:

Author

Language:: English
Keywords:: Humans

Spectrometry, Mass, Electrospray Ionization

Muramidase

Circular Dichroism

Chromatography, High Pressure Liquid

Kinetics

Protein Folding

Amyloid

Spectrometry, Fluorescence

Oxidation-Reduction
Pubs id:: pubs:33171
UUID:: uuid:06229ea6-3bdf-4fbd-9868-f25aa76de87b
Local pid:: pubs:33171
Source identifiers:: 33171
Deposit date:: 2012-12-19

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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