Raffaele Pisano is physicist and Qualified and Habilis (HDR) Lecturer–Researcher of History of physics, History and epistemology of science, e Science & society studies at the University of Lille 1, France. Vice President elected (2011-) of the Inter–Divisional Teaching Commission (Division of Logic, Methodology and Philosophy of Science/International Union for History and Philosophy of Science). Past head of the Research Centre for the Theory and History of Science, University of West Bohemia in Pilsen, Czech Republic. Author of more than one hundred publications in the fields of history and historical epistemology of sciences (physics-mathematics). Recently: Lazare and Sadi Carnot. A Scientific and Filial Relationship (2014, 2nded., Netherland: Springer) with Charles Coulston Gillispie, Princeton University, USA; The Dialectic Relation between Physics and Mathematics in The XIXth Century (2013, Netherland: Springer) co-editor with Evelyne Barbin, University de Nantes, France. Forthcoming: Tartaglia’s Science of Weights and Mechanics in Sixteenth–Century. Selections from Quesiti et inventioni diverse: Books VII–VIII (Netherland: Springer) with Danilo Capecchi, La Sapienza University, Italy; A Bridge between Conceptual Frameworks, Science, Society and Technology Studies (Editor. Netherland: Springer). Newton’s Philosophiae Naturalis Principia Mathematica “Jesuit” Edition: The Tenor of a Huge Work, Accademia Nazionale Lincei-Rendiconti Matematica e Applicazioni 2014, 25:1-32 (with Paolo Bussotti).

More info: fr.linkedin.com/pub/raffaele-pisano/6/a11/a61/

Giuseppe Bellavia is molecular biophysicist and lecturer on physics at University of Lille 1, France. He obtained his PhD at University of Palermo, Italy. His research is mainly focused on proteins in crowded and confined systems, in which residual water plays a key role to mediate the reciprocal protein-sugar interactions. The relationship between structure, dynamics and function of a protein represents the paradigm of biophysics. They converge to the study of the biostability and consequent protein unfolding. Bellavia’s work is integrated in a research line with the aim to obtain a consistent picture of the bioprotection mechanisms through a multiscale approach, from the atomistic to the macroscopic level. The former is obtained by studying the vibrational motions, while the latter from a thermodynamical point of view. In his publications, the solvent dynamics is revealed as a necessary precursor to promote the protein unfolding. The glass transition temperature of the embedding matrix was also found linearly correlated to the protein denaturation temperature. As a consequence, he identified the biostability in the correlation between the collective properties of the matrix and the local properties around the protein.