Published online by Cambridge University Press: 15 February 2011
Silk-like proteins are a topic of long-standing scientific interest and recently are being considered for such uses as high performance fibers [1] and enzyme-immobilizing substrates [2]. The structure of silk (in particular, the metastable silk I form) is critical in understanding the formation and processing of these materials.
Computations provide a useful tool for the detailed modeling of the structures of fibrous proteins. Conformational energy calculations on representative model polypeptides have been used successfully to elucidate the structure of collagen [3]. We have applied this method to the study of the crystalline region of Bombvx mori silk fibroin [4].