Abstract
Extracting a well-designed energy function is important for protein structure evaluation. Knowledge-based potential functions are one type of the energy functions which can be obtained from known protein structures. The pairwise potential between atom types is approximated using Boltzmann’s law which relates the frequency of atom types to its potential. The total energy is approximated as a summation of pairwise potential between the atomic pairs. In the present study, the performance of knowledge-based potential function was assessed based on the strength of interaction between groups of amino acids. The dominant energies involved in the pairwise potentials were revealed by eigenvalue analysis of the matrix, the elements of which represent the energy between amino acids. For this purpose, the matrix including the mean of the energies of residue–residue interaction types was constructed using 500 native protein structures. The matrix has a dominant eigenvalue and amino acids, with LEU, VAL, ILE, PHE, TYR, ALA and TRP having high values along the dominant eigenvector. The results show that the ranking of amino acids is consistent with the power of amino acids in discriminating native structures using K-alphabet reduced model. In the reduced interactions, only amino acids from a subset of all 20 amino acids, along with their interactions are considered to assess the energy. In the K-alphabet reduced model, the reduced structures are constructed based on only the K-amino acid types. The dominant K-alphabet reduced model derived for the k-first amino acids in the list [LEU, VAL, PHE, ILE, TYR, ALA, TRP] of amino acids has the best discrimination of native structure among all possible K-alphabet reduced models. Knowledge-based potentials might be improved with a new strategy.
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The author declares no conflict of interest. This work was financially supported by the Iran National Science Foundation (INSF)(http://en.insf.org/) under Grant number 97003215.
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Mirzaie, M. Discrimination power of knowledge-based potential dictated by the dominant energies in native protein structures. Amino Acids 51, 1029–1038 (2019). https://doi.org/10.1007/s00726-019-02743-0
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DOI: https://doi.org/10.1007/s00726-019-02743-0