Arginine is an important molecule which utilised in industrial, biochemical and medical research to aid in the successful refolding of proteins and to resist the effects of temperature denaturation. Whilst it is emerging as a useful tool, the mechanism by which Arginine interacts with proteins to prevent aggregation is still not fully understood. We aim to complete the first solution-based structural study of Arginine. Our aim is to determine the interactions of Arginine with water and other Arginine molecules. In particular, we are interested in determining the clustering behaviour and answer the following questions: i) Do Arginine molecules associate to form clusters in solution? ii) Do clustered molecules align their methylene groups so as to expose a hydrophobic surface? iii) Are there any other inter-bonds which could be important for preventing protein aggregation?