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Updated: Jul 23, 2025

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

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构建特定于蛋白质结构的旋体库

Algirdas Grybauskas1, Saulius Gražulis1

  • 1Sector of Crystallography and Cheminformatics, Institute of Biotechnology, Life Sciences Center, Vilnius University, 7 Saulėtekio Ave, Vilnius, LT- 10257, Lithuania.

Bioinformatics (Oxford, England)
|July 13, 2023
PubMed
概括

这项研究引入了一种用于预测蛋白质侧链位置的新方法,生成定制二面角图书馆,以提高蛋白质建模和相互作用预测的准确性. 该rotag软件提供了一个更精确的替代标准rotamer库.

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相关概念视频

Protein Organization01:24

Protein Organization

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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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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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Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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