Structural basis for the reactivity of Nitrophorin 7 with diatomic ligands and its interaction with membranes

The present thesis reports exclusively about the main research thread concerning Rhodnius prolixus Nitrophorin 7, a peculiar member of a family of nitric oxide trasporting proteins. This particular protein displays a distinctive behaviour, when compared with the other, better known members of its family, in terms of NO transport and release mechanisms and of interactions with phospholipidic membranes. The computational studies, aimed at clarifying aspects such as the structure of the system of cavities and tunnels inside the protein, the pH-triggered conformational transition, the membrane interaction and its influence on the NO stocking and release, were conducted in collaboration with prof. F. Javier Luque's group (Universitat de Barcelona) and dr. Markus Knipp's group at the Max Planck Institut fà¼r chemische Energiekonversion (Mà¼lheim a. d. Ruhr).