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

• DOI: 10.1126/science.274.5290.1161
• Publication Date: 2002-07-27T09:45:50Z
• Authors: Jochen Balbach; Vincent Forge; Wai Shun Lau; Nico A. J. van Nu...; Keith Brew; Christopher M. Do...
• Keywords: Heteronuclear molecule; Folding (DSP implementation)

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