Post written by Dipanwita Batabyal, UC Irvine, USA.
This research article is from the Henryk Kozlowski group at the University of Wroclaw, Poland and presents thermodynamic and spectroscopic data to investigate the role of methionine residues in copper (II) binding to the non-octarepeat site of the human prion protein (hPrP). The role of methionine residues in Cu(II)/hPrP complexation is controversial and highly debated in the literature. While the spectroscopic data in this work excludes any direct interaction between the sulphur of Met and Cu(II), the thermodynamic data however indicates that Met-109 might contribute to the stability of the complex species.
Thermodynamic and spectroscopic investigation on the role of Met residues in CuII binding to the non-octarepeat site of the human prion protein
Maurizio Remelli, Daniela Valensin, Leonardo Toso, Ewa Gralka, Remo Guerrini, Erika Marzola and Henryk Kozłowski
Metallomics, 2012, Advance Article