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• W1998931888 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." @default.
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• W1998931888 date "1995-07-03" @default.
• W1998931888 modified "2023-09-26" @default.
• W1998931888 title "A pathway for the thermal destabilization of bacteriorhodopsin" @default.
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• W1998931888 doi "https://doi.org/10.1016/0014-5793(95)00570-y" @default.
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