期刊
FEBS LETTERS
卷 576, 期 3, 页码 313-319出版社
WILEY
DOI: 10.1016/j.febslet.2004.09.024
关键词
beta 2-microglobulin; amyloid fibrils; protein misfolding; hydrophobic interaction; guanidine hydrochloride
Although the stability of globular proteins has been studied extensively, that of amyloid fibrils is scarcely characterized. beta(2)-microglobulin (beta2-m) is a major component of the amyloid fibrils observed in patients with dialysis-related amyloidosis. We studied the effects of guanidine hydrochloride on the amyloid fibrils of beta2-m, revealing a cooperative unfolding transition similar to that of the native state. The stability of amyloid fibrils increased on the addition of ammonium sulfate, consistent with a role of hydrophobic interactions. The results indicate that the analysis of unfolding transition is useful to obtain insight into the structural stability of amyloid fibrils. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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