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The previous sections have shown that the three-dimensional coordinates of
a protein structure can be represented in two dimensions with minimal loss
of intramolecular relationships. In particular the relationships between
residues making multiple and important interactions, such as those in
-sheets, are most preserved (see the distance matrices in
Figures 5.4 and 5.6(e)). We have not
defined core residues per se, nor have we devised a means to compare
the cores of analogous structures (as in
Swindellsswindells:cores). In the following section we utilise
the Kohonen self-organising map to extract essential information from both
three-dimensional structural information and one-dimensional sequence
information simultaneously. This is followed by a quantitative analysis of
the suitability of mapped sequence information in fold recognition.