Quantitative prediction of critical amino acid positions for protein folding.
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%.
Thireou
Trias
T
Laboratory of Genetics, Agricultural University of Athens, Athens, Greece.
Atlamazoglou
Vassilios
V
Papandreou
Nikolaos A
NA
Lonquety
Mathieu
M
Chomilier
Jacques
J
Eliopoulos
Elias
E
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
C062612:ABP1 protein, S cerevisiae; D008840:Microfilament Proteins; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins