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- W2164557685 abstract "Statistical potentials have been widely used in protein studies despite the much-debated theoretical basis. In this work, we have applied two physical reference states for deriving the statistical potentials based on protein structure features to achieve zero interaction and orthogonalization. The free-rotating chain-based potential applies a local free-rotating chain reference state, which could theoretically be described by the Gaussian distribution. The self-avoiding chain-based potential applies a reference state derived from a database of artificial self-avoiding backbones generated by Monte Carlo simulation. These physical reference states are independent of known protein structures and are based solely on the analytical formulation or simulation method. The new potentials performed better and yielded higher Z-scores and success rates compared to other statistical potentials. The end-to-end distance distribution produced by the self-avoiding chain model was similar to the distance distribution of protein atoms in structure database. This fact may partly explain the basis of the reference states that depend on the atom pair frequency observed in the protein database. The current study showed that a more physical reference model improved the performance of statistical potentials in protein fold recognition, which could also be extended to other types of applications." @default.
- W2164557685 created "2016-06-24" @default.
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- W2164557685 date "2007-06-01" @default.
- W2164557685 modified "2023-09-30" @default.
- W2164557685 title "A Free-Rotating and Self-Avoiding Chain Model for Deriving Statistical Potentials Based on Protein Structures" @default.
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- W2164557685 doi "https://doi.org/10.1529/biophysj.106.102152" @default.
- W2164557685 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1868969" @default.
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- W2164557685 hasPublicationYear "2007" @default.
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