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Background  Predicting 3-dimensional protein structures from amino-acid sequences is an important unsolved problem in computational structural biology. The problem becomes relatively easier if close homologous proteins have been solved, as high-resolution models can be built by aligning target sequences to the solved homologous structures. However, for sequences without similar folds in the Protein Data Bank (PDB) library, the models have to be predicted from scratch. Progress in the  ab initio  structure modeling is slow. The aim of this study was to extend the TASSER ( t hreading/ asse mbly/ r efinement) method for the  ab initio  modeling and examine systemically its ability to fold small single-domain proteins.    Results  We developed I-TASSER by iteratively implementing the TASSER method, which is used in the folding test of three benchmarks of small proteins. First, data on 16 small proteins (< 90 residues) were used to generate I-TASSER models, which had an average C α -root mean square deviation (RMSD) of 3.8Å, with 6 of them having a C α -RMSD < 2.5Å. The overall result was comparable with the all-atomic ROSETTA simulation, but the central processing unit (CPU) time by I-TASSER was much shorter (150 CPU days vs. 5 CPU hours). Second, data on 20 small proteins (< 120 residues) were used. I-TASSER folded four of them with a C α -RMSD < 2.5Å. The average C α -RMSD of the I-TASSER models was 3.9Å, whereas it was 5.9Å using TOUCHSTONE-II software. Finally, 20 non-homologous small proteins (< 120 residues) were taken from the PDB library. An average C α -RMSD of 3.9Å was obtained for the third benchmark, with seven cases having a C α -RMSD < 2.5Å.    Conclusion  Our simulation results show that I-TASSER can consistently predict the correct folds and sometimes high-resolution models for small single-domain proteins. Compared with other  ab initio  modeling methods such as ROSETTA and TOUCHSTONE II, the average performance of I-TASSER is either much better or is similar within a lower computational time. These data, together with the significant performance of automated I-TASSER server (the Zhang-Server) in the 'free modeling' section of the recent Critical Assessment of Structure Prediction (CASP)7 experiment, demonstrate new progresses in automated  ab initio  model generation. The I-TASSER server is freely available for academic users   .

Ab initio modeling of small proteins by iterative TASSER simulations