| Abstract: | Atomic force microscopy (AFM) has been used to study the noncovalent interactions 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 peptide forming linear rods. The N‐ and C‐terminal domains of the subunit would, therefore, appear to contain regions that interact through noncovalent interactions in the absence of disulfide bond formation. These regions may be of importance in facilitating disulfide bond formation during protein body development. |
