Abstract:
:Escherichia coli phosphofructokinase-2 (Pfk-2) is a homodimer whose subunits consist of a large domain and an additional beta-sheet that provides the interfacial contacts between the subunits, creating a beta-barrel flattened-like structure with the adjacent subunit's beta-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Baez M,Babul Jdoi
10.1016/j.febslet.2009.05.034subject
Has Abstractpub_date
2009-06-18 00:00:00pages
2054-60issue
12eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00405-0journal_volume
583pub_type
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