Abstract
While simple aggregation in solution typically leads to ramified objects, some polymers and proteins form filamentous structures. The aggregation of collagen, a structural protein, from monomers to fibrils was studied by light scattering and atomic force microscopy. The presence of clear, stable intermediates indicates that the assembly proceeds in a modular or hierarchical fashion. Temperature and concentration dependence studies show that the detailed assembly mechanism may change under different conditions.
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