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Science 15 November 1996:
Vol. 274. no. 5290, pp. 1161 - 1163
DOI: 10.1126/science.274.5290.1161
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Reports
Protein Folding Monitored at Individual Residues During a
Two-Dimensional NMR Experiment
Jochen Balbach,
*
Vincent Forge,
Wai Shun Lau,
Nico A. J. van Nuland,
Keith Brew,
Christopher M. Dobson
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
 -lactalbumin. The general approach, however, should be applicable to
the investigation of a wide range of chemical reactions.
J. Balbach, V. Forge, W. S. Lau, N. A. J. van Nuland, C. M. Dobson, Oxford Centre for Molecular Sciences, New Chemistry Laboratory,
University of Oxford, South Parks Road, Oxford OX1 3QT, UK.
K. Brew, Department of Biochemistry and Molecular Biology, University
of Miami School of Medicine, Miami, FL 33101, USA.
*
Present address: Laboratorium für Biochemie,
Universität Bayreuth, D-95440 Bayreuth, Germany.
Present address: CNRS, Unité de Recherche Associée
2096, Section de Biophysique des Proteines et des Membranes, Department de Biologie Cellulaire et Moleculaire, Commissariat a L'Energie Atomique-Centre d'Etudes de Saclay, 91191 Gif-sur-Yvette, France.
To whom correspondence should be addressed.
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- Detection of residue contacts in a protein folding intermediate.
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