Glutathione is a small peptide with a crucial role in living organisms. This molecule is found in Nature in both reduced (GSH) and oxidized (GSSG) forms and a high GSH/GSSG ratio is essential, to the cell. Glutathione is also present in several enzymatic reactions and can be found in many protein structures. As small peptides, these molecules do not have a defined structure in solution and are able to sample a broad conformational space. In addition, both molecules have several titration sites (four in GSH and six in GSSG) and their conformational space is inevitably influenced by pH. Here, we present a detailed conformational study of GSH and GSSG in a range of pH values, together with a full pH titration of these molecules. We performed constant-pH MD simulations of GSH and GSSG at 24 pH values in a total of 14.4 mu s (300 ns per pH value). We obtained the two titration curves and the pK(a) values for all titrable groups with good agreement with experimental data. We also observed that GSH and GSSG have a large conformational variability in solution and their structural preferences are not significantly affected upon binding to proteins. Some exceptions were found and investigated in detail.