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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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High throughput characterization of structural differences between closely related proteins in solution.

Alexander Zaslavsky1, Pedro Madeira, Leonid Breydo

  • 1Analiza, Inc., 3516 Superior Ave., Suite 4407B, Cleveland, OH 44114, USA.

Biochimica Et Biophysica Acta
|November 24, 2012
PubMed
Summary

Protein partitioning in aqueous two-phase systems (ATPS) quantifies subtle 3D structure differences between related proteins. This method offers practical applications for comparative protein analysis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Separation Science

Background:

  • Protein partitioning in aqueous two-phase systems (ATPS) depends on protein-solvent interactions.
  • Understanding these interactions is key to protein characterization.

Purpose of the Study:

  • To describe a method for quantifying 3D structural differences between closely related proteins using ATPS.
  • To explore practical applications of this technique for comparative protein analysis.

Main Methods:

  • Utilizing a set of ATPS with varying compositions.
  • Analyzing protein partitioning behavior across different ATPS conditions.

Main Results:

  • Demonstrated that ATPS partitioning can effectively differentiate between subtle structural variations in proteins.
  • Quantified structural differences based on partitioning coefficients.

Conclusions:

  • ATPS offers a valuable tool for comparative analysis of protein higher-order structures.
  • The described method provides a practical approach for structural characterization.