  Evolution of the amino acid sequences of transthyretin (TTR) can provide
additional information about its dynamics that both complements and extends the
already extensive static structural data. Protein dynamics is largely driven by
interactions between the protein itself and the thin water film that covers it.
Here those interactions are connected to profiles of water waves connecting
domain pivots (hydrophobic extrema), as well as a broad hydrophilic central
hinge region that has evolved to provide human TTR with greater flexibility and
stability. This central region has a density of single mutations related to
amyloid polyneuropathy that is three times higher than other regions.
