We present a simulated annealing-based method for the prediction of the tertiary structures of proteins given knowledge of the secondary structure associated with each amino acid in the sequence. The backbone is represented in a detailed fashion whereas the sidechains and pair-wise interactions are modeled in a simplified way, following the LINUS model of Srinivasan and Rose. A perceptron-based technique is used to optimize the interaction potentials for a training set of three proteins. For these proteins, the procedure is able to reproduce the tertiary structures to below 3 Angstrom in root mean square deviation (rmsd) from the PDB targets. We present the results of tests on twelve other proteins. For half of these, the lowest energy decoy has a rmsd from the native state below 6 Angstrom and, in 9 out of 12 cases, we obtain decoys whose rmsd from the native states are also well below 5 Angstrom.

Assembly of protein tertiary structures from secondary structures using optimized potentials

SENO, FLAVIO;MARITAN, AMOS
2003

Abstract

We present a simulated annealing-based method for the prediction of the tertiary structures of proteins given knowledge of the secondary structure associated with each amino acid in the sequence. The backbone is represented in a detailed fashion whereas the sidechains and pair-wise interactions are modeled in a simplified way, following the LINUS model of Srinivasan and Rose. A perceptron-based technique is used to optimize the interaction potentials for a training set of three proteins. For these proteins, the procedure is able to reproduce the tertiary structures to below 3 Angstrom in root mean square deviation (rmsd) from the PDB targets. We present the results of tests on twelve other proteins. For half of these, the lowest energy decoy has a rmsd from the native state below 6 Angstrom and, in 9 out of 12 cases, we obtain decoys whose rmsd from the native states are also well below 5 Angstrom.
2003
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/2465602
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