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Related Concept Videos

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.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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 polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry
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Published on: May 17, 2016

Identifying Myc interactors.

Romina Ponzielli1, William B Tu, Igor Jurisica

  • 1Ontario Cancer Institute, The Campbell Family Institute for Cancer Research, Toronto, ON, Canada.

Methods in Molecular Biology (Clifton, N.J.)
|September 6, 2013
PubMed
Summary
This summary is machine-generated.

This chapter details co-immunoprecipitation (Co-IP) and in vitro pull-down assays for identifying Myc protein interactions. These methods help validate potential Myc interactors found through in silico screening.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Myc proteins are crucial transcription factors involved in cell growth and proliferation.
  • Understanding Myc's protein-protein interactions is key to elucidating its regulatory functions.
  • Existing methods for identifying protein interactions require detailed protocols for validation.

Purpose of the Study:

  • To provide detailed methodologies for co-immunoprecipitation (Co-IP) and in vitro pull-down assays.
  • To enable researchers to investigate Myc protein interactions within cellular contexts.
  • To offer strategies for screening and validating Myc-interacting proteins.

Main Methods:

  • Co-immunoprecipitation (Co-IP) from various cellular fractions (whole-cell, cytoplasmic, nuclear).
  • In vitro pull-down assays to assess direct and indirect protein-protein interactions.
  • In silico strategies for prioritizing potential Myc interactors.

Main Results:

  • Detailed protocols for performing Co-IP and in vitro pull-down assays are presented.
  • Methods allow for the identification of Myc interacting partners.
  • The assays can distinguish between direct and indirect protein interactions.

Conclusions:

  • Co-IP and in vitro pull-down assays are essential for studying Myc protein interactions.
  • These techniques, combined with in silico screening, provide a robust approach for Myc interactor discovery and validation.