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Updated: Sep 20, 2025

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

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综合拓数据分析和几何深度学习通过量化蛋白质结合口袋来揭示利基

Peiran Jiang1, Jose Lugo-Martinez1

  • 1Ray and Stephanie Lane Computational Biology Department, School of Computer Science, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA.

Journal of computational biology : a journal of computational molecular cell biology
|May 28, 2025
PubMed
概括

这项研究整合了拓数据分析 (TDA) 和几何深度学习 (GDL) 来分析蛋白质口袋. 结合全球和本地结构观点,可以更好地理解酶的功能和分类.

关键词:
几何深度学习的几何深度学习超图是指一个超图.蛋白质结合口袋 结合蛋白质的口袋拓学数据分析数据分析.

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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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Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Ligand Binding Sites

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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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...
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