학술논문
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
Document Type
Academic Journal
Author
Source
Biochemistry. May 18, 1999, Vol. 38 Issue 20, p6419, 9 p.
Subject
Language
ISSN
0006-2960
Abstract
Stopped-flow fluorescence and hydrogen pulse labeling coupled with mass spectrometry were used to study the unfolding and refolding properties of human lysozyme and two amyloidogenic variants Ile56Thr and Asp67His. The unfolding of each protein in 5.4 guanidine hydrochloride (GuHCl) was 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 were ca. 30 and 160 times greater, respectively, than that of the wild type.