| Author | dc.contributor.author | Báez, Mauricio | |
| Author | dc.contributor.author | Babul Cattán, Jorge | es_CL |
| Admission date | dc.date.accessioned | 2011-04-25T16:39:22Z | |
| Available date | dc.date.available | 2011-04-25T16:39:22Z | |
| Publication date | dc.date.issued | 2009-05-22 | |
| Cita de ítem | dc.identifier.citation | FEBS LETTERS, Volume: 583, Issue: 12, Pages: 2054-2060, 2009 | es_CL |
| Identifier | dc.identifier.issn | 0014-5793 | |
| Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/119175 | |
| Abstract | dc.description.abstract | Escherichia coli phosphofructokinase-2 (Pfk-2) is a homodimer whose subunits consist of a large
domain and an additional b-sheet that provides the interfacial contacts between the subunits, creating
a b-barrel flattened-like structure with the adjacent subunit’s b-sheet. To determine how the
structural organization of Pfk-2 determines its stability, the reversible unfolding of the enzyme
was characterized under equilibrium conditions by enzymatic activity, circular dichroism, fluorescence
and hydrodynamic measurements. Pfk-2 undergoes a cooperative unfolding/dissociation process
with the accumulation of an expanded and unstructured monomeric intermediate with a
marginal stability and a large solvent accessibility with respect to the native dimer. | es_CL |
| Patrocinador | dc.description.sponsorship | This work was supported by a grant from the Comisión Nacional
de Investigación Científica y Tecnológica, FONDECYT 1050818,
Chile. M.B. was supported by Facultad de Ciencias, Universidad
de Chile and partially by FONDECYT. | es_CL |
| Lenguage | dc.language.iso | en | es_CL |
| Publisher | dc.publisher | ELSEVIER SCIENCE BV | es_CL |
| Keywords | dc.subject | Reversible unfolding | es_CL |
| Título | dc.title | Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability | es_CL |
| Document type | dc.type | Artículo de revista | |
