The development of human genome project calls for more rapid and accurate protein structure prediction method to assign the structure and function of gene products. Threading has been proved to be successful in protei...The development of human genome project calls for more rapid and accurate protein structure prediction method to assign the structure and function of gene products. Threading has been proved to be successful in protein fold assignment,although difficulties remain for low homologous sequences. We have developed a method for solving the sequence rearrangement problem in threading. By reshuffling secondary elements,protein structures with the same spatial arrangement of secondary structures but different connections can be predicted. This method has been proved to be useful in fold recognition for proteins of different evolutionary origin and converge to the same fold.展开更多
The three-dimensional （3D） structure prediction of proteins ：is an important task in bioinformatics. Finding energy functions that can better represent residue-residue and residue-solvent interactions is a crucial ...The three-dimensional （3D） structure prediction of proteins ：is an important task in bioinformatics. Finding energy functions that can better represent residue-residue and residue-solvent interactions is a crucial way to improve the prediction accu- racy. The widely used contact energy functions mostly only consider the contact frequency between different types of residues; however, we find that the contact frequency also relates to the residue hydrophobic environment. Accordingly, we present an improved contact energy function to integrate the two factors, which can reflect the influence of hydrophobic interaction on the stabilization of protein 3D structure more effectively. Furthermore, a fold recognition （threading） approach based on this energy function is developed. The testing results obtained with 20 randomly selected proteins demonstrate that, compared with common contact energy functions, the proposed energy function can improve the accuracy of the fold template prediction from 20% to 50%, and can also improve the accuracy of the sequence-template alignment from 35% to 65%.展开更多
文摘The development of human genome project calls for more rapid and accurate protein structure prediction method to assign the structure and function of gene products. Threading has been proved to be successful in protein fold assignment,although difficulties remain for low homologous sequences. We have developed a method for solving the sequence rearrangement problem in threading. By reshuffling secondary elements,protein structures with the same spatial arrangement of secondary structures but different connections can be predicted. This method has been proved to be useful in fold recognition for proteins of different evolutionary origin and converge to the same fold.
基金supported by the National Natural Science Foundation of China(No.90203011 and 30370354)the Ministry of Education of China(No.505010 and CG2003-GA002)
文摘The three-dimensional （3D） structure prediction of proteins ：is an important task in bioinformatics. Finding energy functions that can better represent residue-residue and residue-solvent interactions is a crucial way to improve the prediction accu- racy. The widely used contact energy functions mostly only consider the contact frequency between different types of residues; however, we find that the contact frequency also relates to the residue hydrophobic environment. Accordingly, we present an improved contact energy function to integrate the two factors, which can reflect the influence of hydrophobic interaction on the stabilization of protein 3D structure more effectively. Furthermore, a fold recognition （threading） approach based on this energy function is developed. The testing results obtained with 20 randomly selected proteins demonstrate that, compared with common contact energy functions, the proposed energy function can improve the accuracy of the fold template prediction from 20% to 50%, and can also improve the accuracy of the sequence-template alignment from 35% to 65%.
基金supported by National Natural Science Foundation of China(NO.31500673)the Education and Science Foundation for Young teachers of Fujian(JA14049)+1 种基金Start-Up Fund of Fuzhou University(XRC-1336)Science Development Foundation of Fuzhou University(2013-XY-17 and 2014-XY-15)
