| Abstract: | The existence and distribution of vertical, interacting edges on cylindrical surfaces, which were derived from the basic structural features of the collagen molecule, have been examined as a function of the angle θ of the superhelix. Over the range θ = 26°–33° and near θ = 36°, the strongest intermolecular association was detected at 29.95°. This model exhibited three similar, self-interacting edges, separated by approximately 120°. The potential for three similar but nonidentical edges lies in the geometry of the collagen molecule, but the existence of such edges and their ability to self-associate is dependent upon the unique amino acid sequence. The relative strengths of association of each edge with itself and with the other edges are not identical, but the present analysis does not permit a judgment as to whether this variation could result in functional specificity in such interactions. All three chains participate in each edge though their contribution to the relative interaction strength is not identical. These edges showed distinct maxima when displaced past one another by integral intervals of D, where D = 233 residue positions (quarter-stagger). The strongest relative interaction occurs at a displacement of 1D. |
