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Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.

Publication ,  Journal Article
Zhou, P; Wagner, G
Published in: J Biomol NMR
January 2010

Although the rapid progress of NMR technology has significantly expanded the range of NMR-trackable systems, preparation of NMR-suitable samples that are highly soluble and stable remains a bottleneck for studies of many biological systems. The application of solubility-enhancement tags (SETs) has been highly effective in overcoming solubility and sample stability issues and has enabled structural studies of important biological systems previously deemed unapproachable by solution NMR techniques. In this review, we provide a brief survey of the development and successful applications of the SET strategy in biomolecular NMR.We also comment on the criteria for choosing optimal SETs, such as for differently charged target proteins, and recent new developments on NMR-invisible SETs.

Duke Scholars

Published In

J Biomol NMR

DOI

EISSN

1573-5001

Publication Date

January 2010

Volume

46

Issue

1

Start / End Page

23 / 31

Location

Netherlands

Related Subject Headings

  • Thermodynamics
  • Solubility
  • Recombinant Fusion Proteins
  • Proteins
  • Protein Stability
  • Protein Multimerization
  • Protein Engineering
  • Protein Conformation
  • Nuclear Magnetic Resonance, Biomolecular
  • Biophysics
 

Citation

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MLA
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Zhou, P., & Wagner, G. (2010). Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies. J Biomol NMR, 46(1), 23–31. https://doi.org/10.1007/s10858-009-9371-6
Zhou, Pei, and Gerhard Wagner. “Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.J Biomol NMR 46, no. 1 (January 2010): 23–31. https://doi.org/10.1007/s10858-009-9371-6.
Zhou, Pei, and Gerhard Wagner. “Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.J Biomol NMR, vol. 46, no. 1, Jan. 2010, pp. 23–31. Pubmed, doi:10.1007/s10858-009-9371-6.
Journal cover image

Published In

J Biomol NMR

DOI

EISSN

1573-5001

Publication Date

January 2010

Volume

46

Issue

1

Start / End Page

23 / 31

Location

Netherlands

Related Subject Headings

  • Thermodynamics
  • Solubility
  • Recombinant Fusion Proteins
  • Proteins
  • Protein Stability
  • Protein Multimerization
  • Protein Engineering
  • Protein Conformation
  • Nuclear Magnetic Resonance, Biomolecular
  • Biophysics