Protein Folding Monitored at Individual Residues During a Two-Dimensional NMR Experiment

  • Balbach J
  • Forge V
  • Lau W
 et al. 
  • 29


    Mendeley users who have this article in their library.
  • N/A


    Citations of this article.


An approach is described to monitor directly at the level of individual residues the formation of structure during protein folding. A two-dimensional heteronuclear nuclear magnetic resonance (NMR) spectrum was recorded after the rapid initiation of the refolding of a protein labeled with nitrogen-15. The intensities and line shapes of the cross peaks in the spectrum reflected the kinetic time course of the folding events that occurred during the spectral accumulation. The method was used to demonstrate the cooperative nature of the acquisition of the native main chain fold of apo bovine alpha-lactalbumin. The general approach, however, should be applicable to the investigation of a wide range of chemical reactions.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • J. Balbach

  • V. Forge

  • W. S. Lau

  • N. A. J. van Nuland

  • K. Brew

  • C. M. Dobson

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free