Please use this identifier to cite or link to this item: http://rdcb.cbg.ipn.mx/handle/20.500.12273/137
Title: Thermal-unfolding reaction of triosephosphate isomerase from Trypanosoma cruzi
Author: CLAUDIA GUADALUPE BENITEZ CARDOZA
Author ID: info:eu-repo/dai/mx/cvu/25026
Abstract: Thermal denaturation of triosephosphate isomerase from Trypanosoma cruzi was studied by circular dicrhoism and fluorescence spectroscopies. The unfolding transition was found to be highly irreversible even at the very early stages of the reaction. Kinetic studies, allowed us to identify consecutive reactions. Firstly, only the tryptophan environment is altered. Next, changes on the secondary structure and hydrophobic surface exposure measured by 1-anilino-8-naphthalenesulfonate (ANS) binding were observed. Further conformational changes imply additional modifications on the secondary and tertiary structures and release of the hydrophobic dye leading to the formation of the unfolded state that is prone to aggregate.
Issue Date: 1-Sep-2007
License: http://creativecommons.org/about/cc0/
URI: http://rdcb.cbg.ipn.mx/handle/20.500.12273/137
Language: eng
Appears in Collections:Artículos Científicos

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