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ACS Publications. Most Trusted. Most Cited. Most Read
New Knowledge-Based Scoring Function with Inclusion of Backbone Conformational Entropies from Protein Structures
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    New Knowledge-Based Scoring Function with Inclusion of Backbone Conformational Entropies from Protein Structures
    Click to copy article linkArticle link copied!

    • Xinxiang Wang
      Xinxiang Wang
      School of Physics, Huazhong University of Science and Technology, Wuhan, Hubei 430074, P. R. China
    • Di Zhang
      Di Zhang
      School of Physics, Huazhong University of Science and Technology, Wuhan, Hubei 430074, P. R. China
      More by Di Zhang
    • Sheng-You Huang*
      Sheng-You Huang
      School of Physics, Huazhong University of Science and Technology, Wuhan, Hubei 430074, P. R. China
      *E-mail: [email protected]. Phone: +86-27-87543881. Fax: +86-027-87556576.
    Other Access OptionsSupporting Information (1)

    Journal of Chemical Information and Modeling

    Cite this: J. Chem. Inf. Model. 2018, 58, 3, 724–732
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    https://doi.org/10.1021/acs.jcim.7b00601
    Published February 14, 2018
    Copyright © 2018 American Chemical Society

    Abstract

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    Accurate prediction of a protein’s structure requires a reliable free energy function that consists of both enthalpic and entropic contributions. Although considerable progresses have been made in the calculation of potential energies in protein structure prediction, the computation for entropies of protein has lagged far behind, due to the challenge that estimation of entropies often requires expensive conformational sampling. In this study, we have used a knowledge-based approach to estimate the backbone conformational entropies from experimentally determined structures. Instead of conducting computationally expensive MD/MC simulations, we obtained the entropies of protein structures based on the normalized probability distributions of back dihedral angles observed in the native structures. Our new knowledge-based scoring function with inclusion of the backbone entropies, which is referred to as ITScoreDA or ITDA, was extensively evaluated on 16 commonly used decoy sets and compared with 50 other published scoring functions. It was shown that ITDA is significantly superior to the other tested scoring functions in selecting native structures from decoys. The present study suggests the role of backbone conformational entropies in protein structures and provides a way for fast estimation of the entropic effect.

    Copyright © 2018 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.jcim.7b00601.

    • Tables S1–S4 as mentioned in the text (PDF)

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    Cited By

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    This article is cited by 6 publications.

    1. Arghya Chakravorty, Jonathan Higham, Richard H. Henchman. Entropy of Proteins Using Multiscale Cell Correlation. Journal of Chemical Information and Modeling 2020, 60 (11) , 5540-5551. https://doi.org/10.1021/acs.jcim.0c00611
    2. Gang Xu, Qinghua Wang, Jianpeng Ma. OPUS-Fold: An Open-Source Protein Folding Framework Based on Torsion-Angle Sampling. Journal of Chemical Theory and Computation 2020, 16 (6) , 3970-3976. https://doi.org/10.1021/acs.jctc.0c00186
    3. Xinxiang Wang, Sheng-You Huang. Integrating Bonded and Nonbonded Potentials in the Knowledge-Based Scoring Function for Protein Structure Prediction. Journal of Chemical Information and Modeling 2019, 59 (6) , 3080-3090. https://doi.org/10.1021/acs.jcim.9b00057
    4. Ya-Lan Tan, Xunxun Wang, Ya-Zhou Shi, Wenbing Zhang, Zhi-Jie Tan. rsRNASP: A residue-separation-based statistical potential for RNA 3D structure evaluation. Biophysical Journal 2022, 121 (1) , 142-156. https://doi.org/10.1016/j.bpj.2021.11.016
    5. Zhongwang Yu, Yuangen Yao, Haiyou Deng, Ming Yi. ANDIS: an atomic angle- and distance-dependent statistical potential for protein structure quality assessment. BMC Bioinformatics 2019, 20 (1) https://doi.org/10.1186/s12859-019-2898-y
    6. Shiyang Long, Pu Tian. A simple neural network implementation of generalized solvation free energy for assessment of protein structural models. RSC Advances 2019, 9 (62) , 36227-36233. https://doi.org/10.1039/C9RA05168F

    Journal of Chemical Information and Modeling

    Cite this: J. Chem. Inf. Model. 2018, 58, 3, 724–732
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.jcim.7b00601
    Published February 14, 2018
    Copyright © 2018 American Chemical Society

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