A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

Journal Article (Journal Article)

Protein-fusion constructs have been used with great success for enhancing expression of soluble recombinant protein and as tags for affinity purification. Unfortunately the most popular tags, such as GST and MBP, are large, which hinders direct NMR studies of the fusion proteins. Cleavage of the fusion proteins often re-introduces problems with solubility and stability. Here we describe the use of N-terminally fused protein G (B1 domain) as a non-cleavable solubility-enhancement tag (SET) for structure determination of a dimeric protein complex. The SET enhances the solubility and stability of the fusion product dramatically while not interacting directly with the protein of interest. This approach can be used for structural characterization of poorly behaving protein systems, and would be especially useful for structural genomics studies.

Full Text

Duke Authors

Cited Authors

  • Zhou, P; Lugovskoy, AA; Wagner, G

Published Date

  • May 2001

Published In

Volume / Issue

  • 20 / 1

Start / End Page

  • 11 - 14

PubMed ID

  • 11430750

International Standard Serial Number (ISSN)

  • 0925-2738

Digital Object Identifier (DOI)

  • 10.1023/a:1011258906244


  • eng

Conference Location

  • Netherlands