Ontology highlight
ABSTRACT:
SUBMITTER: Malgieri G
PROVIDER: S-EPMC5933289 | biostudies-literature | 2018 Apr
REPOSITORIES: biostudies-literature
Malgieri Gaetano G D'Abrosca Gianluca G Pirone Luciano L Toto Angelo A Palmieri Maddalena M Russo Luigi L Sciacca Michele Francesco Maria MFM Tatè Rosarita R Sivo Valeria V Baglivo Ilaria I Majewska Roksana R Coletta Massimo M Pedone Paolo Vincenzo PV Isernia Carla C De Stefano Mario M Gianni Stefano S Pedone Emilia Maria EM Milardi Danilo D Fattorusso Roberto R
Chemical science 20180301 13
Significant advances in the understanding of the molecular determinants of fibrillogenesis can be expected from comparative studies of the aggregation propensities of proteins with highly homologous structures but different folding pathways. Here, we fully characterize, by means of stopped-flow, T-jump, CD and DSC experiments, the unfolding mechanisms of three highly homologous proteins, zinc binding Ros87 and Ml1<sub>53-149</sub> and zinc-lacking Ml4<sub>52-151</sub>. The results indicate that ...[more]