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Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.

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 ...

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Publication status:
Published

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Publisher copy:
10.1021/bi983037t

Authors


Miranker, A More by this author
Spencer, A More by this author
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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

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