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A pathway for the thermal destabilization of bacteriorhodopsin
S G Taneva1, J M Caaveiro, A Muga
1Department of Biochemistry, University of the Basque Country, Bilbao, Spain.
FEBS Letters
|July 3, 1995
Abstract:
A variety of structural techniques, including IR spectroscopy, reveals that thermal denaturation of bacteriorhodopsin follows a given pathway (successively rearrangement of helical structures, extensive deuterium exchange, and finally protein aggregation) irrespective of heating rate, pH or ionic strength conditions. In all cases, thermal denaturation leads to a 'compact denatured state' which retains a large proportion of ordered structure.