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Quantitative Prediction of Critical Amino Acid Positions for Protein Folding

[ Vol. 16 , Issue. 11 ]


Trias Thireou, Vassilios Atlamazoglou, Nikolaos A. Papandreou, Mathieu Lonquety, Jacques Chomilier and Elias Eliopoulos   Pages 1342 - 1349 ( 8 )


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%.


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


Laboratory of Genetics, Agricultural University of Athens, Iera Odos 75, Athens 118-55, Greece.

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