scispace - formally typeset
G

Giulia Di Rocco

Researcher at University of Modena and Reggio Emilia

Publications -  58
Citations -  1039

Giulia Di Rocco is an academic researcher from University of Modena and Reggio Emilia. The author has contributed to research in topics: Cytochrome c & Heme. The author has an hindex of 15, co-authored 51 publications receiving 902 citations. Previous affiliations of Giulia Di Rocco include Leiden University & Universidade Nova de Lisboa.

Papers
More filters
Journal ArticleDOI

Enamel peptides reveal the sex of the Late Antique ‘Lovers of Modena’

TL;DR: The dimorphic features of the amelogenin protein were exploited to determine the sex of the so-called ‘Lovers of Modena’, two Late Antique individuals whose skeletons were intentionally buried hand-in-hand and were compared to 14 modern and archaeological control samples, confirming the reliability of the ion chromatogram method for sex determination.
Journal ArticleDOI

Enthalpy/entropy compensation phenomena in the reduction thermodynamics of electron transport metalloproteins.

TL;DR: It is concluded that reduction-induced solvent reorganization effects involving the hydration shell of the molecule dominate the reduction thermodynamics in these species, although they have no net effect on the E° values, owing to exact compensation.
Journal ArticleDOI

Electron Transfer Properties and Hydrogen Peroxide Electrocatalysis of Cytochrome c Variants at Positions 67 and 80

TL;DR: The thermodynamic study shows that insertion of His and Ala residues in place of Tyr67 results mainly in differences in protein-solvent interactions at the heme crevice with no relevant effects on the E degrees' values at pH 7.
Journal ArticleDOI

Effects of Mutational (Lys to Ala) Surface Charge Changes on the Redox Properties of Electrode-Immobilized Cytochrome c

TL;DR: The results suggest that the species-dependent orientation of the protein (and thereby of the heme group) toward the negatively charged SAM influences the electrostatic interaction and the resulting E degree' change.
Journal ArticleDOI

Role of Met80 and Tyr67 in the low-pH conformational equilibria of cytochrome c.

TL;DR: Data show that removal of the axial methionine ligand does not significantly alter the mechanism of acidic unfolding and the ranges of stability of low-pH conformers, and underlines the key role played by Tyr67 in stabilizing the three-dimensional structure of cytochrome c by means of the hydrogen bonding network connecting the Ω loops formed by residues 71-85 and 40-57.