The equilibrium unfolding of triosephosphate isomerase from t. cruzi in guanidinium hydrochloride is a four state process. Intrinsic fluorescence studies
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| Formato: | Artículo científico |
| Lenguaje: | en |
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Sociedad Química de México
2004
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| _version_ | 1876442149698928640 |
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| author | Brenda Guadalupe Sánchez Rebollar |
| author_facet | Brenda Guadalupe Sánchez Rebollar |
| contents | The equilibrium unfolding of triosephosphate isomerase from t. cruzi in guanidinium hydrochloride is a four state process. Intrinsic fluorescence studies Brenda Guadalupe Sánchez Rebollar Edgar Vázquez Contreras María Elena Chánez Cárdenas Multidisciplinaria (Ciencias Naturales y Exactas) Triosephoshate isomerase protein folding equilibrium intermediates Equilibrium and kinetic folding pathways of severalhomologous proteins have been studied. Early studies concluded thatthe folding routes of homologous proteins follow fundamentally similarpathways, and that the folding of a certain conformation is conservedthroughout evolution. However, there are examples of homologousproteins that unfold by different routes. Regarding triosephosphateisomerase (TIM), unfolding studies with enzymes from differentsources, have shown: 1) two-state behaviors and 2) more complexprocesses (including two equilibrium-unfolding intermediates andinespecific aggregation), in the transition from de native homodimerto the denatured monomers. In this work, we studied the changes inintrinsic fluorescence of TIM from Trypanosoma cruzi after incubationin guanidinium hydrochloride. Our results show that the reactionis described by a four state process. Finally we discuss the results interms of the heterogeneity observed in TIM denaturation. 2004 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47548417 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.4 Vol.48 |
| format | Artículo científico |
| id | redalyc_47548417 |
| institution | Redalyc |
| language | en |
| publishDate | 2004 |
| publisher | Sociedad Química de México |
| spellingShingle | The equilibrium unfolding of triosephosphate isomerase from t. cruzi in guanidinium hydrochloride is a four state process. Intrinsic fluorescence studies Brenda Guadalupe Sánchez Rebollar Multidisciplinaria (Ciencias Naturales y Exactas) Triosephoshate isomerase protein folding equilibrium intermediates The equilibrium unfolding of triosephosphate isomerase from t. cruzi in guanidinium hydrochloride is a four state process. Intrinsic fluorescence studies Brenda Guadalupe Sánchez Rebollar Edgar Vázquez Contreras María Elena Chánez Cárdenas Multidisciplinaria (Ciencias Naturales y Exactas) Triosephoshate isomerase protein folding equilibrium intermediates Equilibrium and kinetic folding pathways of severalhomologous proteins have been studied. Early studies concluded thatthe folding routes of homologous proteins follow fundamentally similarpathways, and that the folding of a certain conformation is conservedthroughout evolution. However, there are examples of homologousproteins that unfold by different routes. Regarding triosephosphateisomerase (TIM), unfolding studies with enzymes from differentsources, have shown: 1) two-state behaviors and 2) more complexprocesses (including two equilibrium-unfolding intermediates andinespecific aggregation), in the transition from de native homodimerto the denatured monomers. In this work, we studied the changes inintrinsic fluorescence of TIM from Trypanosoma cruzi after incubationin guanidinium hydrochloride. Our results show that the reactionis described by a four state process. Finally we discuss the results interms of the heterogeneity observed in TIM denaturation. 2004 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47548417 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.4 Vol.48 |
| title | The equilibrium unfolding of triosephosphate isomerase from t. cruzi in guanidinium hydrochloride is a four state process. Intrinsic fluorescence studies |
| topic | Multidisciplinaria (Ciencias Naturales y Exactas) Triosephoshate isomerase protein folding equilibrium intermediates |
| url | https://www.redalyc.org/articulo.oa?id=47548417 |