Now showing items 1-2 of 2

    • A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase 

      Jiménez Sandoval, Pedro; Vique Sánchez, José Luis; López Hidalgo, Marisol; Velázquez Juárez, Gilberto; Diaz Quezada, Corina; Arroyo Navarro, Luis Fernando; Montero Morán, Gabriela Margarita; Fattori, Juliana; Díaz Salazar, Alma Jessica; Rudiño Piñera, Enrique; Sotelo Mundo, Rogerio Rafael; Migliorini Figueira, Ana Carolina; Lara González, Samuel; Benítez Cardoza, Claudia Guadalupe; Brieba, Luis G. (Elsevier, 2017)
      "The protozoan parasite Trichomonas vaginalis contains two nearly identical triosephosphate isomerases (TvTIMs) that dissociate into stable monomers and dimerize upon substrate binding. Herein, we compare the role of the ...
    • Self-association of enolase from Trichomonas vaginalis. monomers, dimers, and octamers coexist in solution 

      Mirasol Meléndez, Elibeth; Lima Muñoz, Enrique Jaime; Lara, Víctor Hugo; Brieba de Castro, Luis Gabriel; Lara González, Samuel; Benitez Cardoza, Claudia Guadalupe (American Chemical Society, 2018)
      "We used small-angle X-ray scattering to study the self-association of enolase from Trichomonas vaginalis as a function of the protein concentration and cosolute type. We observed coexisting monomers, dimers, and octamers ...