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Abstract:
Protein folding is a complicated, easily disrupted process, and even after 4 billion years of evolution, protein misfolding and aggregation continue to be major challenges for all living beings. Despite these problems, natural proteins nevertheless represent a best-case group, as in their overwhelming majority polypeptides do not appear to have a folded structure at all. Unsurprisingly, except in viruses, proteins emerged de novo are largely or entirely unstructured. New structured proteins do however emerge continually in nature from pieces of existing proteins. The dominant mechanism for this is repetition and the resulting proteins are almost invariably solenoids of fibers. Here we will review examples of this process at work in the surface proteins of bacteria.
