A novel EDAs based method for HP model protein folding
CEC'09 Proceedings of the Eleventh conference on Congress on Evolutionary Computation
Differential evolution for protein structure prediction using the HP model
IWINAC'11 Proceedings of the 4th international conference on Interplay between natural and artificial computation - Volume Part I
An evolutionary model based on hill-climbing search operators for protein structure prediction
EvoBIO'10 Proceedings of the 8th European conference on Evolutionary Computation, Machine Learning and Data Mining in Bioinformatics
Applied Bionics and Biomechanics
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Determination of the native state of a protein from its amino acid sequence is the goal of protein folding simulations, with potential applications in gene therapy and drug design. To predict a global minimum (GM) structure of a given sequence is a difficult task. A genetic algorithm (GA) is an efficient approach to find lowest-energy conformation for HP lattice model. We have introduced some new operators (symmetric and cornerchange operators) to speed up the searching process and give the result more biology significance. The result shows these new operators improved the success of prediction, compared with standard GA for benchmark HP sequence up to 50 residues