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Biophys J, November 2002, p. 2792-2800, Vol. 83, No. 5

Dynamic Transition Associated with the Thermal Denaturation of a Small Beta Protein

Daniela Russo,* Javier Pérez,dagger Jean-Marc Zanotti,* Michel Desmadril,Dagger and Dominique Duranddagger

 *Laboratoire Léon Brillouin, CE Saclay, 91191 Gif-sur-Yvette Cédex,  dagger Laboratoire pour l'Utilisation du Rayonnement Electromagnétique, Université Paris-Sud, 91898 Orsay Cédex, and  Dagger Laboratoire de Modélisation et d'Ingéniere des Protéines, Université Paris-Sud, 91405 Orsay Cédex, France

We studied the temperature dependence of the picosecond internal dynamics of an all-beta protein, neocarzinostatin, by incoherent quasielastic neutron scattering. Measurements were made between 20°C and 71°C in heavy water solution. At 20°C, only 33% of the nonexchanged hydrogen atoms show detectable dynamics, a number very close to the fraction of protons involved in the side chains of random coil structures, therefore suggesting a rigid structure in which the only detectable diffusive movements are those involving the side chains of random coil structures. At 61.8°C, although the protein structure is still native, slight dynamic changes are detected that could reflect enhanced backbone and beta -sheet side-chain motions at this higher temperature. Conversely, all internal dynamics parameters (amplitude of diffusive motions, fraction of immobile scatterers, mean-squared vibration amplitude) rapidly change during heat-induced unfolding, indicating a major loss of rigidity of the beta -sandwich structure. The number of protons with diffusive motion increases markedly, whereas the volume occupied by the diffusive motion of protons is reduced. At the half-transition temperature (T = 71°C) most of backbone and beta -sheet side-chain hydrogen atoms are involved in picosecond dynamics.

Biophys J, November 2002, p. 2792-2800, Vol. 83, No. 5
© 2002 by the Biophysical Society   0006-3495/02/11/2792/09  $2.00


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