A retroprotein has exactly the same sequence as a naturally-occurring protein, except that the direction in which the polypeptide backbone runs through the protein is exactly the opposite of what it was in the first place. In this paper, we show that spherical hollow structures formed by retroHSP12.6 can associate into long fiber-like structures, fused by polypeptide material from amorphous aggregate deposits. The data presented in this paper suggests (i) that bead-shaped aggregates can associate to form fibers, and (ii) that amorphous aggregate deposits can birth amyloid aggregates and act as nurseries for their growth.  

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