The dynamical behavior of the Bombyx mori silk fibroin chain and of absorbed water in silk fiber, film, and powder has been studied by H-1 pulsed nuclear magnetic resonance (NMR). Segmental motions do not occur and only the rapid rotation of the methyl groups of alanine residues is observed from -120 to 130-degrees-C. This is independent of the conformation or form of the silk fibroin samples. Magnetization of dry silk fibroin by the solid-echo method shows a single Gaussian decay, while two components are observed in the solid-echo signals of films containing 6-10 w/w% water. An immobile component with a T2 value of 11-mu-s is attributed to silk fibroin, and the mobile component to bound water. The T2 of the latter varies from 50 to 200-mu-s, depending on the sample. The dynamical behavior of water trapped in the film is discussed on the basis of these T2 values.