- Abstract:
-
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) is well described as a two-state process, but the rates of unfolding of the Ile56Thr variant and the Asp67His variant in 5.4 M GuHCl are ca. 30 and 160 times greater, respectively, than that of the ...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi983037t
-
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- Journal:
- Biochemistry
- Volume:
- 38
- Issue:
- 20
- Pages:
- 6419-6427
- Publication date:
- 1999-05-05
- DOI:
- EISSN:
-
1520-4995
- ISSN:
-
0006-2960
- URN:
-
uuid:b414ba7a-9a61-4315-8cee-b7fd3c2a7552
- Source identifiers:
-
59217
- Local pid:
- pubs:59217
- Copyright date:
- 1999
Journal article
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.
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