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Related Experiment Video

Updated: Jun 18, 2026

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

Protein identification using Sorcerer 2 and SEQUEST.

Deborah H Lundgren1, Harryl Martinez, Michael E Wright

  • 1Department of Cell Biology, Center for Vascular Biology, University of Connecticut Health Center, Farmington, Connecticut, USA.

Current Protocols in Bioinformatics
|December 4, 2009
PubMed
Summary
This summary is machine-generated.

Sage-N

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Last Updated: Jun 18, 2026

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Area of Science:

  • Proteomics
  • Bioinformatics
  • Computational Biology

Background:

  • Protein identification from complex mixtures is crucial in proteomics.
  • Existing tools require integrated systems for efficient data analysis.
  • The SEQUEST algorithm is a widely used search engine for protein identification.

Purpose of the Study:

  • To present a protocol for processing mass spectrometric data using Sage-N's Sorcerer 2.
  • To describe result analysis with the Trans-Proteomic Pipeline (TPP) and Scaffold software.
  • To provide an overview of the SEQUEST algorithm and its enhancements in Sorcerer-SEQUEST.

Main Methods:

  • Utilizing Sage-N's Sorcerer 2 for integrated data analysis.
  • Processing mass spectrometric data through Sorcerer 2.
  • Analyzing identified proteins using TPP and Scaffold.

Main Results:

  • Sorcerer 2 facilitates comprehensive protein identification and characterization.
  • The system integrates the SEQUEST algorithm for protein search.
  • The protocol details data processing, analysis, and interpretation.

Conclusions:

  • Sorcerer 2 offers an integrated solution for proteomic data analysis.
  • Understanding SEQUEST algorithm and data filtering is key for accurate interpretation.
  • The presented protocol aids users in running Sorcerer and interpreting SEQUEST results.