Atomic force microscopy (AFM) has been used to study the non-covalent inter
actions of alkylated HMW subunit 1Dx5 and a M-r 58,000 peptide derived from
the central repetitive domain. Both protein and peptide align side-by-side
to form fibrils, the HMW subunit forming a branched network, and the pepti
de forming linear rods. The N- and C-terminal domains of the subunit would,
therefore, appear to contain regions that interact through noncovalent int
eractions in the absence of disulfide bond formation. These regions may be
of importance in facilitating disulfide bond formation during protein body
development.