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simulink simscape multibody dynamic simulation  (MathWorks Inc)


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    MathWorks Inc simulink simscape multibody dynamic simulation
    Simulink Simscape Multibody Dynamic Simulation, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 96/100, based on 902 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/simulink simscape multibody dynamic simulation/product/MathWorks Inc
    Average 96 stars, based on 902 article reviews
    simulink simscape multibody dynamic simulation - by Bioz Stars, 2026-05
    96/100 stars

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    Image Search Results


    Identification, characterization of AsSDR1 and AsSDR2. (a) Saccharomyces cerevisiae AS2.346 transformation reaction; (b) Phylogenetic analysis of carbonyl reductases. The phylogenetic tree was constructed based on the alignment of full amino acid sequences. All analyzed sequences of reductase enzymes were retrieved from GenBank and SGD; (c) Biotransformation reaction of recombination E. coli .

    Journal: Synthetic and Systems Biotechnology

    Article Title: Identification, characterization, and application of an NADPH-dependent carbonyl reductase in Saccharomyces cerevisiae AS2.346 for improving production of (13R,17S)-ethyl secol

    doi: 10.1016/j.synbio.2025.04.016

    Figure Lengend Snippet: Identification, characterization of AsSDR1 and AsSDR2. (a) Saccharomyces cerevisiae AS2.346 transformation reaction; (b) Phylogenetic analysis of carbonyl reductases. The phylogenetic tree was constructed based on the alignment of full amino acid sequences. All analyzed sequences of reductase enzymes were retrieved from GenBank and SGD; (c) Biotransformation reaction of recombination E. coli .

    Article Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

    Techniques: Transformation Assay, Construct

    Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

    Journal: Synthetic and Systems Biotechnology

    Article Title: Identification, characterization, and application of an NADPH-dependent carbonyl reductase in Saccharomyces cerevisiae AS2.346 for improving production of (13R,17S)-ethyl secol

    doi: 10.1016/j.synbio.2025.04.016

    Figure Lengend Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

    Article Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

    Techniques: Binding Assay

    Optimal Reaction Conditions for AsSDR1 and AsSDR2. (a) Purifed enzymes were reacted at different temperatures and assayed at various temperatures from 20 to 50 °C; (b) Purified enzymes were mixed with different buffers and assayed at various pH values, from 3.0 to 10.0. The values provided are the means of three independent replicates.

    Journal: Synthetic and Systems Biotechnology

    Article Title: Identification, characterization, and application of an NADPH-dependent carbonyl reductase in Saccharomyces cerevisiae AS2.346 for improving production of (13R,17S)-ethyl secol

    doi: 10.1016/j.synbio.2025.04.016

    Figure Lengend Snippet: Optimal Reaction Conditions for AsSDR1 and AsSDR2. (a) Purifed enzymes were reacted at different temperatures and assayed at various temperatures from 20 to 50 °C; (b) Purified enzymes were mixed with different buffers and assayed at various pH values, from 3.0 to 10.0. The values provided are the means of three independent replicates.

    Article Snippet: Molecular Dynamics Simulation Results of AsSDR1 and AsSDR2. (a) Protein-substrate MD distance of AsSDR1 and AsSDR2; (b) diagram of the protein-substrate binding patterns of AsSDR1; (c) diagram of the protein-substrate binding patterns of AsSDR2.

    Techniques: Purification