Proteins, under native conditions, fold to specific 3D struc- tures according to their 1D amino acid sequence, which in turn is defined by the genetic code. The specific shape of a folded protein is a strong indicator of its function in the cell. The mechanisms involved in protein folding are not well understood and predicting the final conformation of a folded protein from its amino acid sequence alone is not yet achievable despite extensive research efforts, both theoretical and experimental. The protein folding process may be viewed as an emergent phenomenon, a result of underlying physics controlling the interaction of amino acids with their local environment, leading to the complex global fold. In this spirit we present a model for investigating protein folding using open L-systems, local rewriting rules with environmental interaction.