title: Structural reorganization renders enhanced metalloprotein stability.
abstract: The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural interconversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.
authors: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, EAN 2785-572, Oeiras, Portugal.
authors: Hugo M
authors: HM
authors: Botelho
authors: Cláudio M
authors: CM
authors: Gomes
mesh_terms: D045286:Desulfovibrio gigas; D007501:Iron / Q000378:metabolism; D011489:Protein Denaturation; D055550:Protein Stability; D012416:Rubredoxins / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis
chemical_list: D012416:Rubredoxins; D007501:Iron