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Updated: Jun 5, 2025

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Published on: July 25, 2013

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BindCraft:功能性蛋白质结合剂的一次性设计

Martin Pacesa, Lennart Nickel, Christian Schellhaas

    bioRxiv : the preprint server for biology
    |December 16, 2024
    PubMed
    概括

    BindCraft是一个新的计算管道,设计具有高成功率的蛋白质结合剂. 这种自动化方法实现了对不同目标的纳米分子亲和力,推动了治疗和生物技术的蛋白质设计.

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    An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA07:55

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    相关概念视频

    Conserved Binding Sites01:49

    Conserved Binding Sites

    Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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    Ligand Binding and Linkage00:49

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    Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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    Ligand Binding Sites02:40

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    Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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    Protein-protein Interfaces02:04

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    The Equilibrium Binding Constant and Binding Strength02:18

    The Equilibrium Binding Constant and Binding Strength

    The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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    Protein Complexes with Interchangeable Parts01:57

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    Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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