The Experts below are selected from a list of 179388 Experts worldwide ranked by ideXlab platform

Joshua S. Yuan - One of the best experts on this subject based on the ideXlab platform.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Abstract Background Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. Results HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Conclusion Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

Ugur Uzuner - One of the best experts on this subject based on the ideXlab platform.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Abstract Background Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. Results HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Conclusion Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

Sanmin Liu - One of the best experts on this subject based on the ideXlab platform.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Abstract Background Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. Results HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Conclusion Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

Lantao Liu - One of the best experts on this subject based on the ideXlab platform.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Abstract Background Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. Results HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Conclusion Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

Weibing Shi - One of the best experts on this subject based on the ideXlab platform.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.

  • Enzyme Structure dynamics of xylanase I from Trichoderma longibrachiatum
    BMC Bioinformatics, 2010
    Co-Authors: Ugur Uzuner, Weibing Shi, Lantao Liu, Sanmin Liu, Susie Y. Dai, Joshua S. Yuan
    Abstract:

    Abstract Background Enzyme dynamics has recently been shown to be crucial for Structure-function relationship. Among various Structure dynamics analysis platforms, HDX (hydrogen deuterium exchange) mass spectrometry stands out as an efficient and high-throughput way to analyze protein dynamics upon ligand binding. Despite the potential, limited research has employed the HDX mass spec platform to probe regional Structure dynamics of Enzymes. In particular, the technique has never been used for analyzing cell wall degrading Enzymes. We hereby used xylanase as a model to explore the potential of HDX mass spectrometry for studying cell wall degrading Enzymes. Results HDX mass spectrometry revealed significant intrinsic dynamics for the xylanase Enzyme. Different regions of the Enzymes are differentially stabilized in the apo Enzyme. The comparison of substrate-binding Enzymes revealed that xylohexaose can significantly stabilize the Enzyme. Several regions including those near the reaction centres were significantly stabilized during the xylohexaose binding. As compared to xylohexaose, xylan induced relatively less protection in the Enzyme, which may be due to the insolubility of the substrate. The Structure relevance of the Enzyme dynamics was discussed with reference to the three dimensional Structure of the Enzyme. HDX mass spectrometry revealed strong dynamics-function relevance and such relevance can be explored for the future Enzyme improvement. Conclusion Ligand-binding can lead to the significant stabilization at both regional and global level for Enzymes like xylanase. HDX mass spectrometry is a powerful high-throughput platform to identify the key regions protected during the ligand binding and to explore the molecular mechanisms of the Enzyme function. The HDX mass spectrometry analysis of cell wall degrading Enzymes has provided a novel platform to guide the rational design of Enzymes.