As discussed in the literature [18-21], non-local patterns (where bit-patterns are one type of non-local patterns,) in contact maps can effectively capture the secondary structure of proteins. Our previous work [6,7] demonstrated that by characterizing the spatial relationship among the above described bit-patterns, one can construct structural signatures for proteins of different classes or folds. In the context of protein folding, we have observed that the above-defined bit-patterns are also capable of capturing a wide range of local 3D structural motifs. They can even approximately measure the strength of secondary structure propensity in a conformation. For instance, we have identified bit-patterns that correspond to "premature" α-helices and native-like α-helices respectively. Henceforth, we refer to the 3D structure formed by all the participating residues of a bit-pattern as the 3D motif of the bit-pattern. The relationship between bit-patterns and 3D motifs will be further discussed in the next section.