Quantitative Prediction of Critical Amino Acid Positions for Protein Folding

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

Affiliation:

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%.

Cite this article as:

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

DOI https://dx.doi.org/10.2174/092986609789353673	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305