Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.
The unfolding and refolding properties of human lysozyme and two amyloidogenic variants (Ile56Thr and Asp67His) have been studied by stopped-flow fluorescence and hydrogen exchange pulse labeling coupled with mass spectrometry. The unfolding of each protein in 5.4 M guanidine hydrochloride (GuHCl) i...
Main Authors: | Canet, D, Sunde, M, Last, A, Miranker, A, Spencer, A, Robinson, C, Dobson, C |
---|---|
Format: | Journal article |
Language: | English |
Published: |
1999
|
Similar Items
-
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
by: Canet, D, et al.
Published: (2002) -
The solution dynamics of amyloidogenic Asp67His variant of human lysozyme: Insights from hydrogen exchange
by: Canet, D, et al.
Published: (2000) -
Is lysozyme variant Thr70Asn amyloidogenic?
by: Booth, DR, et al.
Published: (2001) -
Conformational dynamics and protein unfolding in lysozyme amyloidosis
by: Sunde, M, et al.
Published: (1999) -
Investigation of non-covalent interactions of amyloidogenic human lysozyme variants and camelid antibodies
by: Caddy, G, et al.
Published: (2002)