G-protein coupled receptors (GPCRs) are the largest family of membrane-bound receptors and are associated with a wide range of diseases. To enable rational design of compounds for therapeutic purposes, the difficulties associated with crystallisation of wild-type GPCRs must be overcome. Current methods involve addition of thermostabilising mutations and/or incorporation of stabilising protein domains. This is exemplified in a recently solved structure of the neurotensin receptor 1 (NTS₁), which contains six thermostabilising mutations and T4-lysozyme replacing an intracellular loop. An alternative approach uses directed evolution to engineer highly detergent stable GPCR mutants. The crystal structures of several NTS₁ variants engineered in this way have been recently solved. We are developing computational methods for the design of detergent stable GPCRs using algorithms that incorporate consensus sequence information, preservation of binding site residues and evolutionarily coupled sites. We envisage that this will enhance the production, crystallisation and structure determination of GPCRs. Here we explore the flexibility and dynamics of existing NTS₁ structures using molecular dynamics simulations. Further, we attempt to understand how the manner by which stabilisation is achieved alters the dynamics of NTS₁ and the possible impact this has upon the equilibrium between inactive and active states.