The kinetics of conformation transition of the
Bombyx mori silk fibroin membrane from poorly
defined to the well-ordered state was analyzed for
the first time. Using FTIR spectroscopy, independent
measures of the b-sheet conformation could
be analyzed simultaneously with the loss of random
coil structure. As would be expected for the
molecular rearrangement of such a large protein
system, the kinetics of formation of the ‘perfected’
state is slow, and multiple intermediate
states are indicated. However, the initial formation
of b-sheet structure, which accounts for 50%
of the conformation transition mechanism, may
be rapid. Further study is required to understand
this interesting and complex conformation transi