Two notably similar proteins follows different unfolding pathways

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Autor principal: Edgar Vázquez Contreras
Formato: Artículo científico
Lenguaje:en
Publicado: Sociedad Química de México 2002
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author Edgar Vázquez Contreras
author_facet Edgar Vázquez Contreras
contents Two notably similar proteins follows different unfolding pathways Edgar Vázquez Contreras María Elena Chánez Cárdenas Multidisciplinaria (Ciencias Naturales y Exactas) proteines fluorescence unfolding pathway Triosephosphate isomerase three dimensional structures The amino acid sequences and the three dimensional structuresof triosephosphate isomerase from the parasites Trypanosomabruceiand Trypanosoma cruzi, are markedly similar. In spite of thesestructural similarities, we found that the equilibrium unfolding pathwayof both enzymes induced by guanidinium hydrochloride is different,as showed by alterations in intrinsic fluorescence of tryptophanresidues. This behavior is possibly related with the differentreactivity that these enzymes presents against derivatizing cysteineresidues agents. 2002 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47546307 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.3 Vol.46
format Artículo científico
id redalyc_47546307
institution Redalyc
language en
publishDate 2002
publisher Sociedad Química de México
spellingShingle Two notably similar proteins follows different unfolding pathways
Edgar Vázquez Contreras
Multidisciplinaria (Ciencias Naturales y Exactas)
proteines
fluorescence
unfolding pathway
Triosephosphate isomerase
three dimensional structures
Two notably similar proteins follows different unfolding pathways Edgar Vázquez Contreras María Elena Chánez Cárdenas Multidisciplinaria (Ciencias Naturales y Exactas) proteines fluorescence unfolding pathway Triosephosphate isomerase three dimensional structures The amino acid sequences and the three dimensional structuresof triosephosphate isomerase from the parasites Trypanosomabruceiand Trypanosoma cruzi, are markedly similar. In spite of thesestructural similarities, we found that the equilibrium unfolding pathwayof both enzymes induced by guanidinium hydrochloride is different,as showed by alterations in intrinsic fluorescence of tryptophanresidues. This behavior is possibly related with the differentreactivity that these enzymes presents against derivatizing cysteineresidues agents. 2002 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47546307 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.3 Vol.46
title Two notably similar proteins follows different unfolding pathways
topic Multidisciplinaria (Ciencias Naturales y Exactas)
proteines
fluorescence
unfolding pathway
Triosephosphate isomerase
three dimensional structures
url https://www.redalyc.org/articulo.oa?id=47546307