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相关概念视频

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conservation of Protein Domains02:26

Conservation of Protein Domains

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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相关实验视频

Updated: May 7, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

从未确定的宏分子结构数据中恢复一个代表性的构造组合.

Konstantin Berlin, Carlos A Castañeda, Dina Schneidman-Duhovny

    Journal of the American Chemical Society
    |October 8, 2013
    PubMed
    概括

    我们开发了Sparse Ensemble Selection (SES),一种通过分析多种构造来确定蛋白质和核酸结构的新方法. SES准确地揭示了分子结构如何随着pH等条件的变化而改变,有助于理解生物相互作用.

    科学领域:

    • 生物物理学的生物物理.
    • 结构生物学 结构生物学
    • 计算生物学 计算生物学

    背景情况:

    • 由于域之间的连接器,巨分子灵活性需要将分子表示为构成的集合,而不是单个结构.
    • 实验数据代表了多个形状的平均值,这使得直接解卷是一个不合时宜的问题.
    • 稀疏近似和压缩传感为从未确定系统中恢复信息提供了解决方案.

    研究的目的:

    • 开发一种新的方法,即Sparse Ensemble Selection (SES),用于从有限的实验数据中恢复构造组合.
    • 在不同的pH条件下,将SES应用于与Lys48结合的duibiquitin,以获得具有代表性的 conformational ensembles.
    • 为了验证和比较SES的结果与现有的方法和实验数据.

    主要方法:

    • 设计了稀疏组合选择 (SES) 方法,灵感来自稀疏近似和压缩传感.
    • 使用在多个pH值下测量的残余二极合数据,将SES应用于与Lys48相关的二极.
    • 对NMR化学转移扰动数据进行了验证,并将其与最大的结果进行了比较.

    主要成果:

    • SES准确地回收了Lys48结合的duibiquitin的代表性形状组合.
    • 该方法重现并量化了主要diubiquitin构成的pH依赖性.

    更多相关视频

    A Protocol for Computer-Based Protein Structure and Function Prediction
    16:41

    A Protocol for Computer-Based Protein Structure and Function Prediction

    Published on: November 3, 2011

    相关实验视频

    Last Updated: May 7, 2026

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
    09:51

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

    Published on: July 16, 2017

    A Protocol for Computer-Based Protein Structure and Function Prediction
    16:41

    A Protocol for Computer-Based Protein Structure and Function Prediction

    Published on: November 3, 2011

  • SES发现了预先组织的较少的人口构造,用于绑定duibiquitin受体.

    • 结论:

    • 与以前的方法相比,SES提供了一种更普遍,更准确的方法来确定构造组合.
    • 鉴定到的形状提供了对聚比基介导受体识别机制的见解.
    • SES广泛适用于各种实验可观测物,可用状态数据的线性组合来表示.