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Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo‐dimer with topologically interlinked chains
Author(s) -
Aguirre César,
Goto Yuji,
Costas Miguel
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12041
Subject(s) - dimer , monomer , chemistry , crystallography , dissociation (chemistry) , protein folding , folding (dsp implementation) , biophysics , polymer , biochemistry , biology , organic chemistry , electrical engineering , engineering
Understanding the mechanisms as to how interlinked proteins entangle and fold is a challenge. PaSdsA1 sulfatase is a homo‐dimer containing two zinc atoms per monomer. The monomer chains are interlinked in a dimerization domain. To study the unfolding pathways denaturation experiments were performed. In the native protein three forms coexist in chemical equilibrium, each with a different number of zinc atoms. In the chemical unfolding of the holo‐dimers the entanglement of the chains is preserved and acts as a ‘folding seed’, allowing the unfolding process to be reversible. Thermal irreversible unfolding of the holo‐dimers favours dissociation, producing monomers that are SDS ‐stabilized. The thermal unfolding of these monomers is reversible. However, it is not possible to form dimers from unfolded monomers.