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Local structure formation in simulations of two small proteins.

ABSTRACT: Massively parallel all-atom, explicit solvent molecular dynamics simulations were used to explore the formation and existence of local structure in two small alpha-helical proteins, the villin headpiece and the helical fragment B of protein A. We report on the existence of transient helices and combinations of helices in the unfolded ensemble, and on the order of formation of helices, which appears to largely agree with previous experimental results. Transient local structure is observed even in the absence of overall native structure. We also calculate sets of residue-residue pairs that are statistically predictive of the formation of given local structures in our simulations.

SUBMITTER: Jayachandran G

PROVIDER: S-EPMC1931413 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature

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Local structure formation in simulations of two small proteins.

Jayachandran Guha G Vishal V V García Angel E AE Pande Vijay S VS

Journal of structural biology 20061011 3

Massively parallel all-atom, explicit solvent molecular dynamics simulations were used to explore the formation and existence of local structure in two small alpha-helical proteins, the villin headpiece and the helical fragment B of protein A. We report on the existence of transient helices and combinations of helices in the unfolded ensemble, and on the order of formation of helices, which appears to largely agree with previous experimental results. Transient local structure is observed even in ...[more]

PMID: 17098444

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Project description:BackgroundPredicting 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 (threading/assembly/refinement) method for the ab initio modeling and examine systemically its ability to fold small single-domain proteins.ResultsWe 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 Calpha-root mean square deviation (RMSD) of 3.8A, with 6 of them having a Calpha-RMSD < 2.5A. 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 Calpha-RMSD < 2.5A. The average Calpha-RMSD of the I-TASSER models was 3.9A, whereas it was 5.9A using TOUCHSTONE-II software. Finally, 20 non-homologous small proteins (< 120 residues) were taken from the PDB library. An average Calpha-RMSD of 3.9A was obtained for the third benchmark, with seven cases having a Calpha-RMSD < 2.5A.ConclusionOur 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 http://zhang.bioinformatics.ku.edu/I-TASSER.

Dataset Information

Local structure formation in simulations of two small proteins.

Publications

Local structure formation in simulations of two small proteins.

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