  The notion of energy landscapes provides conceptual tools for understanding
the complexities of protein folding and function. Energy Landscape Theory
indicates that it is much easier to find sequences that satisfy the "Principle
of Minimal Frustration" when the folded structure is symmetric (Wolynes, P. G.
Symmetry and the Energy Landscapes of Biomolecules. Proc. Natl. Acad. Sci.
U.S.A. 1996, 93, 14249-14255). Similarly, repeats and structural mosaics may be
fundamentally related to landscapes with multiple embedded funnels. Here we
present analytical tools to detect and compare structural repetitions in
protein molecules. By an exhaustive analysis of the distribution of structural
repeats using a robust metric we define those portions of a protein molecule
that best describe the overall structure as a tessellation of basic units. The
patterns produced by such tessellations provide intuitive representations of
the repeating regions and their association towards higher order arrangements.
We find that some protein architectures can be described as nearly periodic,
while in others clear separations between repetitions exist. Since the method
is independent of amino acid sequence information we can identify structural
units that can be encoded by a variety of distinct amino acid sequences.
