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