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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

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An analysis pipeline for the inference of protein-protein interaction networks

Ronald C Taylor1, Mudita Singhal, Don S Daly

  • 1Computational Sciences and Mathematics Division, Pacific Northwest National Laboratory (US Department of Energy), Richland, WA 99352, USA. ronald.taylor@pnl.gov

International Journal of Data Mining and Bioinformatics
|January 8, 2010
PubMed

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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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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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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 polypeptide...
Protein-Protein Interfaces02:04

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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 polypeptide...