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using libdock  (Dassault Systemes)

 
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    Structured Review

    Dassault Systemes using libdock
    ( a ) Probabilities of interaction between polyglutamine peptides and 26 potential surfaces of Ku70 are shown as <t>LibDock</t> scores expected by Discovery Studio. ( b ) Image showing the simulation of the interaction of hexa-glutamine (6Q) at site 4 of Ku70 expected by Discovery Studio. ( c ) LibDock scores (scores for expected binding affinity) of various lengths of polyglutamine peptides in a binding simulation with site 4. ( d ) The 20 polypeptides with the highest LibDock scores for binding to site 4. 7H had a higher score than did polyglutamine of various lengths (polyQs). ( e ) LibDock scores of various lengths of polyhistidine peptides for simulations of binding at site 4.
    Using Libdock, supplied by Dassault Systemes, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/using libdock/product/Dassault Systemes
    Average 90 stars, based on 1 article reviews
    using libdock - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "Identification of hepta-histidine as a candidate drug for Huntington’s disease by in silico-in vitro- in vivo -integrated screens of chemical libraries"

    Article Title: Identification of hepta-histidine as a candidate drug for Huntington’s disease by in silico-in vitro- in vivo -integrated screens of chemical libraries

    Journal: Scientific Reports

    doi: 10.1038/srep33861

    ( a ) Probabilities of interaction between polyglutamine peptides and 26 potential surfaces of Ku70 are shown as LibDock scores expected by Discovery Studio. ( b ) Image showing the simulation of the interaction of hexa-glutamine (6Q) at site 4 of Ku70 expected by Discovery Studio. ( c ) LibDock scores (scores for expected binding affinity) of various lengths of polyglutamine peptides in a binding simulation with site 4. ( d ) The 20 polypeptides with the highest LibDock scores for binding to site 4. 7H had a higher score than did polyglutamine of various lengths (polyQs). ( e ) LibDock scores of various lengths of polyhistidine peptides for simulations of binding at site 4.
    Figure Legend Snippet: ( a ) Probabilities of interaction between polyglutamine peptides and 26 potential surfaces of Ku70 are shown as LibDock scores expected by Discovery Studio. ( b ) Image showing the simulation of the interaction of hexa-glutamine (6Q) at site 4 of Ku70 expected by Discovery Studio. ( c ) LibDock scores (scores for expected binding affinity) of various lengths of polyglutamine peptides in a binding simulation with site 4. ( d ) The 20 polypeptides with the highest LibDock scores for binding to site 4. 7H had a higher score than did polyglutamine of various lengths (polyQs). ( e ) LibDock scores of various lengths of polyhistidine peptides for simulations of binding at site 4.

    Techniques Used: Binding Assay



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    using libdock  (Dassault Systemes)
    90
    Dassault Systemes using libdock
    ( a ) Probabilities of interaction between polyglutamine peptides and 26 potential surfaces of Ku70 are shown as <t>LibDock</t> scores expected by Discovery Studio. ( b ) Image showing the simulation of the interaction of hexa-glutamine (6Q) at site 4 of Ku70 expected by Discovery Studio. ( c ) LibDock scores (scores for expected binding affinity) of various lengths of polyglutamine peptides in a binding simulation with site 4. ( d ) The 20 polypeptides with the highest LibDock scores for binding to site 4. 7H had a higher score than did polyglutamine of various lengths (polyQs). ( e ) LibDock scores of various lengths of polyhistidine peptides for simulations of binding at site 4.
    Using Libdock, supplied by Dassault Systemes, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/using libdock/product/Dassault Systemes
    Average 90 stars, based on 1 article reviews
    using libdock - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    ( a ) Probabilities of interaction between polyglutamine peptides and 26 potential surfaces of Ku70 are shown as LibDock scores expected by Discovery Studio. ( b ) Image showing the simulation of the interaction of hexa-glutamine (6Q) at site 4 of Ku70 expected by Discovery Studio. ( c ) LibDock scores (scores for expected binding affinity) of various lengths of polyglutamine peptides in a binding simulation with site 4. ( d ) The 20 polypeptides with the highest LibDock scores for binding to site 4. 7H had a higher score than did polyglutamine of various lengths (polyQs). ( e ) LibDock scores of various lengths of polyhistidine peptides for simulations of binding at site 4.

    Journal: Scientific Reports

    Article Title: Identification of hepta-histidine as a candidate drug for Huntington’s disease by in silico-in vitro- in vivo -integrated screens of chemical libraries

    doi: 10.1038/srep33861

    Figure Lengend Snippet: ( a ) Probabilities of interaction between polyglutamine peptides and 26 potential surfaces of Ku70 are shown as LibDock scores expected by Discovery Studio. ( b ) Image showing the simulation of the interaction of hexa-glutamine (6Q) at site 4 of Ku70 expected by Discovery Studio. ( c ) LibDock scores (scores for expected binding affinity) of various lengths of polyglutamine peptides in a binding simulation with site 4. ( d ) The 20 polypeptides with the highest LibDock scores for binding to site 4. 7H had a higher score than did polyglutamine of various lengths (polyQs). ( e ) LibDock scores of various lengths of polyhistidine peptides for simulations of binding at site 4.

    Article Snippet: We retrieved the structure of Ku70 (ID: PD0220) from the Protein Data Bank (PDB) ( http://www.rcsb.org/pdb/explore/explore.do?structureid=1JEY ) and screened 3,010,121 chemicals in Chemical Available Purchase (CAP) 2006 (Dassault Systems BIOVIA Cooperation, San Diego) using LibDock.

    Techniques: Binding Assay