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Related Concept Videos

Protein Networks02:26

Protein Networks

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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...
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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
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Thermal proteome profiling for interrogating protein interactions.

André Mateus1, Nils Kurzawa1,2, Isabelle Becher1

  • 1Genome Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.

Molecular Systems Biology
|March 6, 2020
PubMed
Summary
This summary is machine-generated.

Thermal proteome profiling (TPP) measures changes in protein stability using mass spectrometry. This technique reveals protein interactions and drug targets in various biological contexts.

Keywords:
drug discoverymetabolitesprotein complexesproteomicsthermal proteome profiling

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Area of Science:

  • Biochemistry
  • Proteomics
  • Chemical Biology

Background:

  • Proteins undergo denaturation and insolubilization when exposed to heat.
  • Protein thermal stability is altered by interactions with small molecules, nucleic acids, proteins, and post-translational modifications.

Purpose of the Study:

  • To present Thermal Proteome Profiling (TPP) as a method for studying protein interactions and drug targets.
  • To highlight the versatility of TPP across in vitro, in situ, and in vivo systems.

Main Methods:

  • Utilizes multiplexed quantitative mass spectrometry-based proteomics.
  • Monitors the melting profiles of thousands of proteins simultaneously.
  • Assesses changes in protein thermal stability.

Main Results:

  • Successfully applied to identify drug targets and off-targets.
  • Enabled the study of protein-metabolite and protein-protein interactions.
  • Provides insights into protein state and interactions within their native context.

Conclusions:

  • TPP offers a unique, proteome-wide view of protein behavior.
  • Facilitates the study of fundamental biological processes and their mechanisms.
  • A powerful tool for drug discovery and understanding cellular mechanisms.