Computer simulations aimed at structure prediction of supersecondary motifs in proteins.
It is well established that protein structures are more conserved than protein sequences. One-third of all known protein structures can be classified into ten protein folds, which themselves are composed mainly of alpha-helical hairpin, beta hairpin, and betaalphabeta supersecondary structural elements. In this study, we explore the ability of a recent Monte Carlo-based procedure to generate the 3D structures of eight polypeptides that correspond to units of supersecondary structure and three-stranded antiparallel beta sheet. Starting from extended or misfolded compact conformations, all Monte Carlo simulations show significant success in predicting the native topology using a simplified chain representation and an energy model optimized on other structures. Preliminary results on model peptides from nucleotide binding proteins suggest that this simple protein folding model can help clarify the relation between sequence and topology.
Forcellino
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F
Information Génétique et Structurale, UMR 1889 CNRS, Marseille, France.
Derreumaux
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P
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D003198:Computer Simulation; D019077:Helix-Turn-Helix Motifs; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009010:Monte Carlo Method; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017510:Protein Folding
D010455:Peptides