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three-dimensional structures of both the wild-type and mutant pigt  (Accelrys)

 
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    Structured Review

    Accelrys three-dimensional structures of both the wild-type and mutant pigt
    Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed <t>using</t> <t>BIOVIA</t> Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in <t>PIGT</t> across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.
    Three Dimensional Structures Of Both The Wild Type And Mutant Pigt, supplied by Accelrys, 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/product/three-dimensional+structures+of+both+the+wild-type+and+mutant+pigt/pmc11943126-186-8-15?v=Accelrys
    Average 90 stars, based on 1 article reviews
    three-dimensional structures of both the wild-type and mutant pigt - by Bioz Stars, 2026-08
    90/100 stars

    Images

    1) Product Images from "A Novel Homozygous Missense Variant of PIGT Related to Multiple Congenital Anomalies-Hypotonia Seizures Syndrome 3 with Elevated of Serum ALP Level in a Thai Newborn Patient"

    Article Title: A Novel Homozygous Missense Variant of PIGT Related to Multiple Congenital Anomalies-Hypotonia Seizures Syndrome 3 with Elevated of Serum ALP Level in a Thai Newborn Patient

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms26062790

    Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed using BIOVIA Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in PIGT across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.
    Figure Legend Snippet: Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed using BIOVIA Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in PIGT across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.

    Techniques Used: Comparison, Mutagenesis



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    three-dimensional structures of both the wild-type and mutant pigt  (Accelrys)
    90
    Accelrys three-dimensional structures of both the wild-type and mutant pigt
    Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed <t>using</t> <t>BIOVIA</t> Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in <t>PIGT</t> across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.
    Three Dimensional Structures Of Both The Wild Type And Mutant Pigt, supplied by Accelrys, 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/product/three-dimensional+structures+of+both+the+wild-type+and+mutant+pigt/pmc11943126-186-8-15?v=Accelrys
    Average 90 stars, based on 1 article reviews
    three-dimensional structures of both the wild-type and mutant pigt - by Bioz Stars, 2026-08
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed using BIOVIA Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in PIGT across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.

    Journal: International Journal of Molecular Sciences

    Article Title: A Novel Homozygous Missense Variant of PIGT Related to Multiple Congenital Anomalies-Hypotonia Seizures Syndrome 3 with Elevated of Serum ALP Level in a Thai Newborn Patient

    doi: 10.3390/ijms26062790

    Figure Lengend Snippet: Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed using BIOVIA Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in PIGT across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.

    Article Snippet: The three-dimensional structures of both the wild-type and mutant PIGT (PDB: 7wld) were visualized using BIOVIA software [ ].

    Techniques: Comparison, Mutagenesis