Quantitative Prediction of Critical Amino Acid Positions for Protein Folding

Trias      Thireou; Vassilios      Atlamazoglou; Nikolaos   A.   Papandreou; Mathieu      Lonquety; Jacques      Chomilier; Elias      Eliopoulos

doi:10.2174/092986609789353673

Abstract

The MIR algorithm provides an ab initio prediction of a proteins core residues. An improved version, the MIR2, is presented and validated on 3203 proteins from PDB. Structures are decomposed in Closed Loops, their limits constituting the observed core residues. They are predicted by MIR2 with an accuracy approaching 80%.

Keywords: Protein folding, monte carlo method, lattice simulation, folding nucleus, hydrophobic core

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Protein & Peptide Letters

Title: Quantitative Prediction of Critical Amino Acid Positions for Protein Folding

Volume: 16 Issue: 11

Author(s): Trias Thireou, Vassilios Atlamazoglou, Nikolaos A. Papandreou, Mathieu Lonquety, Jacques Chomilier and Elias Eliopoulos

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Keywords: Protein folding, monte carlo method, lattice simulation, folding nucleus, hydrophobic core

Abstract: The MIR algorithm provides an ab initio prediction of a proteins core residues. An improved version, the MIR2, is presented and validated on 3203 proteins from PDB. Structures are decomposed in Closed Loops, their limits constituting the observed core residues. They are predicted by MIR2 with an accuracy approaching 80%.

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Thireou Trias, Atlamazoglou Vassilios, Papandreou A. Nikolaos, Lonquety Mathieu, Chomilier Jacques and Eliopoulos Elias, Quantitative Prediction of Critical Amino Acid Positions for Protein Folding, Protein & Peptide Letters 2009; 16 (11) . https://dx.doi.org/10.2174/092986609789353673