Abstract
This thesis work focuses on the study of protein though the use of high pressure. There are three main points subject that are being inquired here. The first is the study of cooperativity and folding landscape of a repeat protein (Anp32a) though the use high pressure denaturation at different temperatures. The second concerns the investigation of the determinant of thermal expansivity in the folded state of protein using high pressure NMR, and the well characterized Staphylococcal Nuclease (SNase) and some of its mutants. Finally, a last article on the pressure stability of the model mini protein Tryptophan cage variant Tc5b by a combination of high pressure NMR and full atomic replica exchange simulations.