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10.1016/j.jmgm.2020.107650

http://scihub22266oqcxt.onion/10.1016/j.jmgm.2020.107650
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32707520!7346800!32707520
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suck abstract from ncbi


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pmid32707520      J+Mol+Graph+Model 2020 ; 100 (ä): 107650
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  • Identification of correlated inter-residue interactions in protein complex based on the fragment molecular orbital method #MMPMID32707520
  • Tanaka S; Watanabe C; Honma T; Fukuzawa K; Ohishi K; Maruyama T
  • J Mol Graph Model 2020[Nov]; 100 (ä): 107650 PMID32707520show ga
  • A theoretical scheme to systematically describe correlated (network-like) interactions between molecular fragments is proposed within the framework of the fragment molecular orbital (FMO) method. The method is mathematically based on the singular value decomposition (SVD) of the inter-fragment interaction energy (IFIE) matrix obtained by the FMO calculation, and can be applied to a comprehensive description of protein-protein interactions in the context of molecular recognition. In the present study we apply the proposed method to a complex of measles virus hemagglutinin and human SLAM receptor, thus finding a usefulness for efficiently eliciting the correlated interactions among the amino-acid residues involved in the two proteins. Additionally, collective interaction networks by amino-acid residues important for mutation experiments can be clearly visualized.
  • |*Amino Acids[MESH]
  • |*Proteins[MESH]


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