title: Quantitative prediction of critical amino acid positions for protein folding.
abstract: The MIR algorithm provides an ab initio prediction of a protein's 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%.
authors.affiliation: Laboratory of Genetics, Agricultural University of Athens, Athens, Greece.
authors.forename: Trias
authors.initials: T
authors.lastname: Thireou
authors.forename: Vassilios
authors.initials: V
authors.lastname: Atlamazoglou
authors.forename: Nikolaos A
authors.initials: NA
authors.lastname: Papandreou
authors.forename: Mathieu
authors.initials: M
authors.lastname: Lonquety
authors.forename: Jacques
authors.initials: J
authors.lastname: Chomilier
authors.forename: Elias
authors.initials: E
authors.lastname: Eliopoulos
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D030562:Databases, Protein; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism; D009010:Monte Carlo Method; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D015203:Reproducibility of Results; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: C062612:ABP1 protein, S cerevisiae; D008840:Microfilament Proteins; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins