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All roads lead to Rome? The multiple pathways of protein folding Abstract Recent studies have found that protein folding reactions often proceed through two or more kinetically distinct pathways. In at least some cases, the observed folding intermediates act as kinetic traps, slowing the rate at which folding is completed. These findings have important implications for understanding how proteins fold in vitro and in vivo. Introduction Efforts to understand how proteins adopt their native three-dimensional structure have been strongly influenced by two observations. The first, due to Anfinsen and coworkers [1], is that proteins can fold spontaneously on a physiological timescale. The second, due to Levinthal [2], is that there are vastly too many conformations open to a protein for all of the possible states to be sampled. These observations seem, on the face of it, to be mutually exclusive. To resolve this paradox, it was proposed that proteins fold via specific pathways....

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