Reliable prediction of protein thermostability change upon double mutation from amino acid sequence.
The accurate prediction of protein stability change upon mutation is one of the important issues for protein design. In this work, we have focused on the stability change of double mutations and systematically analyzed the wild-type and mutant residues, patterns in amino acid sequence and locations of mutants. Based on the sequence information of wild-type, mutant and three neighboring residues, we have presented a weighted decision table method (WET) for predicting the stability changes of 180 double mutants obtained from thermal (DeltaDeltaG) denaturation. Using 10-fold cross-validation test, our method showed a correlation of 0.75 between experimental and predicted values of stability changes, and an accuracy of 82.2% for discriminating the stabilizing and destabilizing mutants.
Huang
Liang-Tsung
LT
Department of Computer Science and Information Engineering, Mingdao University, Changhua 523, Taiwan.
Gromiha
M Michael
MM
D000595:Amino Acid Sequence; D000596:Amino Acids; D020407:Internet; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry; D009154:Mutation / Q000235:genetics*; D017354:Point Mutation / Q000235:genetics; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D012372:ROC Curve; D012997:Solvents; D013696:Temperature
D000596:Amino Acids; D050505:Mutant Proteins; D011506:Proteins; D012997:Solvents