Forced folding and structural analysis of metastable proteins. Academic Article uri icon


  • A significant fraction of the proteins encoded by the human and other genomes appears to be significantly unfolded in vitro. This will undoubtedly hamper attempts to characterize their structure by classical crystallographic or solution NMR methods. Here we show that encapsulation of a metastable protein within the restricted volume a reverse micelle can be used to force fold the protein and allow its characterization by modern methods of NMR spectroscopy. This may have significant utility in the context of structural proteomics. In addition, variation of the inner volume of the reverse micelle can be used to probe the character of the manifold of unfolded states.

published proceedings

  • J Am Chem Soc

altmetric score

  • 1

author list (cited authors)

  • Peterson, R. W., Anbalagan, K., Tommos, C., & Wand, A. J.

citation count

  • 62

complete list of authors

  • Peterson, Ronald W||Anbalagan, Karthik||Tommos, Cecilia||Wand, A Joshua

publication date

  • August 2004