A new possibility of predicting short disordered regions (loops) at a small window size (three amino acid residues) by the FoldUnfold program is described. As demonstrated with the example of three G proteins, FoldUnfold predicted almost all existing loops at the positions fitting well the X-ray structural data. The loops predicted in the Ras p21 structure were classified into two types. The loops of the first type display high Debye-Waller factor values, characteristic of the so-called functional loops (flexible loops). The second-type loops had lower Debye-Waller factor values and, consequently, were regarded as the loops connecting secondary structure elements (rigid loops). Comparison of the results predicted by FoldUnfold with the predictions of other programs (PONDR, RONN, DisEMBL, PreLINK, IUPred, GlobPlot 2, and FoldIndex) demonstrated that the first program was much better in predicting the positions of short loops. FoldUnfold made it possible to solve the problem difficult for the other programs, that is, to determine the boundary between the ordered and disordered regions in proteins with a large fraction of disordered regions, exemplified by the ubiquitin-like domain. In particular, FoldUnfold predicted a boundary between the ordered and disordered regions at residues 30 and 31, whereas the other programs predicted the boundary in the range of 28-70 amino acid residues.