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Related Concept Videos

Proteomics01:33

Proteomics

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.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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 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...
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...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Complementary proteomic analysis of protein complexes.

Todd M Greco1, Yana Miteva, Frank L Conlon

  • 1Department of Molecular Biology, Princeton University, Princeton, NJ, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 8, 2012
PubMed
Summary
This summary is machine-generated.

This study presents a new proteomic method for analyzing protein complexes, improving the understanding of cellular signaling and macromolecular assemblies. The optimized approach enhances protein identification and functional analysis in complex biological samples.

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Area of Science:

  • Proteomics
  • Molecular Biology
  • Cellular Signaling

Background:

  • Protein complexes are crucial for cellular functions.
  • Understanding their dynamic regulation is key to elucidating signaling pathways.
  • Existing proteomic methods have limitations in characterizing complex or immunoisolated samples.

Purpose of the Study:

  • To develop and optimize a complementary proteomic approach for the characterization of immunoisolated protein complexes.
  • To provide robust workflows for sample preparation, method development, and data analysis.
  • To enable confident identification and functional analysis of proteins within macromolecular assemblies.

Main Methods:

  • Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was employed.
  • Complementary sample preparation workflows were developed.
  • Detailed high-performance liquid chromatography (HPLC) and mass spectrometry method development steps were provided.
  • A bioinformatic workflow for peptide/protein identification and gene ontology analysis was established.

Main Results:

  • The protocol enables confident peptide and protein identification.
  • Unbiased functional gene ontology analysis provides insights into complex functions.
  • The method is adaptable for analyzing complex samples from whole cell or tissue proteomes, including Xenopus.
  • Optimized workflows address variations in protein complexity, abundance, and properties.

Conclusions:

  • This optimized proteomic approach enhances the characterization of immunoisolated protein complexes.
  • The provided workflows facilitate detailed molecular and cellular signaling analysis.
  • The protocol is versatile and extendable to complex biological samples for broader proteomic studies.