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High-throughput Gene Tagging in Trypanosoma brucei
11:26

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Published on: August 12, 2016

The better tag remains unseen.

Florian G Durst1, Horng Der Ou, Frank Löhr

  • 1Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, and Cluster of Excellence Macromolecular Complexes (CEF), University of Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt am Main, Germany

Journal of the American Chemical Society
|October 22, 2008
PubMed
Summary

Preparing high-quality protein samples is essential for nuclear magnetic resonance (NMR) spectroscopy. This study introduces a modular tag system to improve protein expression, purification, and solubility for NMR structure determination.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Spectroscopy

Background:

  • Protein structure determination using nuclear magnetic resonance (NMR) spectroscopy requires high-quality protein samples.
  • Achieving high protein concentration and good sample behavior is a critical challenge.

Purpose of the Study:

  • To present a novel system of modular tags for enhanced protein sample preparation.
  • To facilitate high-level expression, sophisticated purification, and improved solubility of proteins for NMR.

Main Methods:

  • Development of two expression constructs incorporating a modular tag system.
  • Utilization of the specific binding between human calmodulin (hCaM) and calmodulin binding peptide (CBP) for purification.
  • Minimization of additional resonances introduced by the tags.

Main Results:

  • The modular tag system enables high-level protein expression.
  • It allows for sophisticated purification of full-length proteins.
  • The system enhances protein solubility while minimizing spectral interference.

Conclusions:

  • The presented modular tag system is effective for preparing well-behaved, highly concentrated protein samples for NMR.
  • This approach simplifies and improves the process of protein structure determination via NMR spectroscopy.