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Equilibrium and kinetic folding pathways of several homologous proteins have been studied. Early studies concluded that the folding routes of homologous proteins follow fundamentally similar pathways, and that the folding of a certain conformation is conserved throughout evolution. However, there are examples of homologous proteins that unfold by different routes. Regarding triosephosphate isomerase (TIM), unfolding studies with enzymes from different sources, have shown: 1) two-state behaviors and 2) more complex processes (including two equilibrium-unfolding intermediates and inespecific aggregation), in the transition from de native homodimer to the denatured monomers. In this work, we studied the changes in intrinsic fluorescence of TIM from Trypanosoma cruzi after incubation in guanidinium hydrochloride. Our results show that the reaction is described by a four state process. Finally we discuss the results in terms of the heterogeneity observed in TIM denaturation.

Palabras clave: Triosephoshate isomerase, protein folding equilibrium intermediates.
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Universidad Autónoma del Estado de México
Sistema de Información Científica Redalyc ®
Versión 3.0 | 2017
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