A pathway for the thermal destabilization of bacteriorhodopsin.
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.
Taneva
S G
SG
Department of Biochemistry, University of the Basque Country, Bilbao, Spain.
Caaveiro
J M
JM
Muga
A
A
Goñi
F M
FM
D001436:Bacteriorhodopsins / Q000737:chemistry*; D019617:Halobacterium salinarum; D006358:Hot Temperature; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D001436:Bacteriorhodopsins