相关实验视频

Updated: Jan 13, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

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用MutPred-PPI预测误解变异的相互作用特异性蛋白质-蛋白质相互作用干扰

Ross Stewart1, Florent Laval2,3,4,5,6,7,8, Georges Coppin2,3,4,6

  • 1Khoury College of Computer Sciences, Northeastern University, Boston, MA, USA.

bioRxiv : the preprint server for biology
|January 7, 2026
PubMed
概括

MutPred-PPI预测了遗传变异如何破坏蛋白质与蛋白质相互作用 (PPI),超过现有的工具. 这种计算方法有助于通过识别误解变体的特定相互作用效应来理解疾病机制.

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相关概念视频

Protein-protein Interfaces02:04

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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Protein Networks02:26

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Conserved Binding Sites01:49

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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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Covalently Linked Protein Regulators

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