Light-induced denaturation of bacteriorhodopsin from a high-temperature unfolding intermediate state
نویسندگان
چکیده
منابع مشابه
Thermodynamics of denaturant-induced unfolding of a protein that exhibits variable two-state denaturation.
Free energy changes (DeltaG(degrees)(N-->D)) obtained by denaturant-induced unfolding using the linear extrapolation method (LEM) are presumed to reflect the stability differences between native (N) and denatured (D) species in the absence of denaturant. It has been shown that with urea and guanidine hydrochloride (GdnHCl) some proteins exhibit denaturant-independent (DeltaG(degrees)(N-->D)). B...
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Bacteriorhodopsin (bR) trimers naturally form two-dimensional hexagonal crystals in purple membrane (PM), which make it very stable. However, the dnaturation of bR was found to occur during a very narrow pH range when the pH was increased above 12.0, as indicated by inactivation of the photochemical cycle observed by flash photolysis kinetic spectra. Here, atomic force microscopy was used to st...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2001
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.41.s180_2