Browsing by Author "ffa359c7-f670-43b5-8cae-60bb633ebc29"
Now showing items 1-6 of 6
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Báez, Mauricio; Wilson, Christian A.M.; Ramírez Sarmiento, César A.; Guixé Leguía, Victoria Cristina; Babul Cattán, Jorge (2012)Folding studies have been focused mainly on small, single-domain proteins or isolated single domains of larger proteins. However, most of the proteins present in biological systems are composed of multiple domains, and to ...
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Báez, Mauricio; Preller, Ana; Ureta, Tito (Academic Press Inc., 2003)Frog oocyte glycogen synthase properties differ significantly under in vitro or in vivo conditions. The Kmapp for UDP-glucose in vivo was 1.4mM (in the presence or absence of glucose-6-P). The in vitro value was 6mM and ...
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Ramírez Sarmiento, César A.; Báez, Mauricio; Wilson, Christian A.M.; Babul Cattán, Jorge; Komives, Elizabeth; Guixé Leguía, Victoria Cristina (2013)Phosphofructokinase-2 is a dimeric enzyme that undergoes cold denaturation following a highly cooperative N2 2I mechanism with dimer dissociation and formation of an expanded monomeric intermediate. Here, we use intrinsic ...
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Báez, Mauricio; Rodríguez, Patricio H.; Babul Cattán, Jorge; Guixé Leguía, Victoria Cristina (2003)Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with pyrene maleimide (PM) results in a rapid inactivation of the enzyme. The loss of enzyme activity correlates with the incorporation of 2 mol of PM/mol of ...
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Cabrera Paucar, Ricardo; Báez, Mauricio; Pereira, Humberto M.; Caniuguir, André S.; Garratt, Richard C.; Babul Cattán, Jorge (2011)Substrate inhibition by ATP is a regulatory feature of the phosphofructokinases isoenzymes from Escherichia coli (Pfk-1 and Pfk-2). Under gluconeogenic conditions, the loss of this regulation in Pfk-2 causes substrate ...
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Ramírez Sarmiento, César A.; Báez, Mauricio; Zamora, Ricardo A.; Balasubramaniam, Deepa; Babul Cattán, Jorge; Komives, Elizabeth; Guixé Leguía, Victoria Cristina (Biophysical Society, 2015)© 2015 Biophysical Society. Escherichia coli phosphofructokinase-2 (Pfk-2) is an obligate homodimer that follows a highly cooperative three-state folding mechanism N<inf>2</inf> → 2I → 2U. The strong coupling ...