Proteins are known to denature in high concentrations of compounds such as urea or guanidinium chloride. However, the mechanism by which urea and guanidinium chloride destabilizes proteins is not yet known, despite many decades of reasearch. Attempts have been made to understand protein denaturation on a thermodynamic level as well as on a molecular level. The long term goal in the field is to merge the results of these two types of studies into one mechanism that covers both the microscopic and the macroscopic level. In this text we firstly review thermodynamic studies as well as spectroscopic and computer simulation studies of chemical denaturation. The results of the different types of studies is then merged together in order to find a consistent view on chemical denaturation. In contrast to common belief in the field, a high degree of consensus is found between the different studies and a molecular mechanism of urea-induced protein denaturation can therefore be proposed.