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SISTEMA INTEGRAL DE INFORMACIÓN ACADÉMICA - PÚBLICO
Título del libro: Molecular Biology Of Protein Folding, Pt B Título del capítulo: The Folding Pathway of Triosephosphate Isomerase
Autores UNAM: EDGAR VAZQUEZ CONTRERAS;
Autores externos: Idioma: InglésAño de publicación: 2008Resumen:
Triosephosphate isomerase (TIM) is a widely studied enzyme. Their ubiquity, efficient catalytic activity, and its (beta/alpha)(8) barrel three-dimensional conformation, make this enzyme an excellent model to perform almost any kind of research. In this chapter, TIM folding pathway studies are reviewed. These results show that even the native conformation is almost the same for all the species so far analyzed and that the percentage of identity in their primary is higher than 70%, the unfolding pathway is not the same to all of them. The characteristics of the available TIMs are analyzed, their kinetic and equilibrium unfolding studies in different denaturants (urea, guanidine hydrochloride, temperature, and pressure), the reversibility of the processes, the models and energetic of the conformers in the pathway, as well as other properties of the unfolding intermediates are discussed. The interesting case of these homologous proteins is discussed in terms of their folding nature, the (b
