Predicting Protein Interactions by Brownian Dynamics Simulations.

We present a newly adapted Brownian-Dynamics (BD)-based protein docking method for predicting native protein complexes. The approach includes global BD conformational sampling, compact complex selection, and local energy minimization. In order to reduce the computational costs for energy evaluations...

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Publicado en:Journal of Biomedicine & Biotechnology Vol. 2012; pp. 1 - 12
Autores principales: Xuan-Yu Meng, Yu Xu, Hong-Xing Zhang, Mezei, Mihaly, Meng Cui
Formato: algorithm pictorial research tables/charts Journal Article
Publicado: Wiley-Blackwell 2012
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 2012
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      pub: Wiley-Blackwell
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        atl: Predicting Protein Interactions by Brownian Dynamics Simulations.
      aug:
        au:
          Xuan-Yu Meng
          Yu Xu
          Hong-Xing Zhang
          Mezei, Mihaly
          Meng Cui
        affil: Department of Physiology and Biophysics, Virginia Commonwealth University, 1220 East Broad Street, P.O. Box 980551, Richmond, VA 23298, USA; State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023, China
      sug:
        subj:
          Computer Simulation Methods
          Metabolism Evaluation
          Biochemical Phenomena Evaluation
          Molecular Probe Techniques Methods
          Proteins Physiology
          Algorithms
          Physics
          Electricity
          Models, Statistical
          Data Analysis Software
          Descriptive Statistics
          Cluster Analysis
          Funding Source
      ab: We present a newly adapted Brownian-Dynamics (BD)-based protein docking method for predicting native protein complexes. The approach includes global BD conformational sampling, compact complex selection, and local energy minimization. In order to reduce the computational costs for energy evaluations, a shell-based grid force field was developed to represent the receptor protein and solvation effects. The performance of this BD protein docking approach has been evaluated on a test set of 24 crystal protein complexes. Reproduction of experimental structures in the test set indicates the adequate conformational sampling and accurate scoring of this BD protein docking approach. Furthermore, we have developed an approach to account for the flexibility of proteins, which has been successfully applied to reproduce the experimental complex structure from the structure of two unbounded proteins. These results indicate that this adapted BD protein docking approach can be useful for the prediction of protein-protein interactions.
      pubtype: Academic Journal
      doctype:
        algorithm
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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