text: The fact that the binding motif appears as a "triplet" of the conserved TxT repeat, as well as the observation that blastp queries have returned no viable matches, has led some researchers to suggest that RiAFP represents a new type of AFP – one that differs from the heavily studied TmAFP (from T. molitor), DcAFP (from D. canadensis), and CfAFP (from C. fumiferana). On the basis of these observations, it has been predicted that the need for insect AFPs came about after insect evolutionary divergence, much like the evolution of fish AFPs; thus, different AFPs most likely evolved in parallel from adaptations to cold (environmental) stress. As a result, homology modelling with TmAFP, DcAFP, or CfAFP would prove to be fruitless.
  Secondary structure modelling algorithms have determined that the internal repeats are spaced sufficiently to tend towards β-strand configuration; no helical regions include the conserved repeats; and all turn regions are located at the ends of β-strand regions. These data suggest that RiAFP is a well-folded β-helical protein, having six β-strand regions consisting of 13-amino acids (including one TxTxTxT binding motif) per strand.
  Primary crystallographic studies, have been published on a RiAFP crystal (which diffracted to 1.3Å resolution) in the trigonal space group P321 (or P321), with unit-cell parameters a = b = 46.46, c = 193.21Å.