Abstract
The dynamics of hydrated proteins and of protein crystals can be studied within a wide temperature range, since the water of hydration does not crystallize at low temperature. Instead it turns into an amorphous glassy state below 200 K. Extending the temperature range facilitates the spectral separation of different molecular processes. The conformational motions of proteins show an abrupt enhancement near 180 K, which has been called a “dynamical transition”. In this contribution various aspects of the transition are critically reviewed: the role of the instrumental resolution function in extracting displacements from neutron elastic scattering data and the question of the appropriate dynamic model, discrete transitions between states of different energy versus continuous diffusion inside a harmonic well, are discussed. A decomposition of the transition involving two motional components is performed: rotational transitions of methyl groups and small scale librations of side-chains, induced by water at the protein surface. Both processes create an enhancement of the observed amplitude. The onset occurs, when their time scale becomes compatible with the resolution of the spectrometer. The reorientational rate of hydration water follows a super-Arrhenius temperature dependence, a characteristic feature of a dynamical transition. It occurs only with hydrated proteins, while the torsional motion of methyl groups takes place also in the dehydrated or solvent-vitrified system. Finally, the role of fast hydrogen bond fluctuations contributing to the amplitude enhancement is discussed.
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Acknowledgments
This work was supported by a grant of the Deutsche Forschungsgemeinschaft within the SFB 533, light-induced processes in biopolymers. Excellent technical support by the instrument responsibles including the Institut Laue Langevin and numerous discussions with Prof. Wolfgang Götze are gratefully acknowleded. The NMR experiments were performed by Prof. Franz Fujara.
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Advanced neutron scattering and complementary techniques to study biological systems. Contributions from the meetings, “Neutrons in Biology”, STFC Rutherford Appleton Laboratory, Didcot, UK, 11–13 July and “Proteins At Work 2007”, Perugia, Italy, 28–30 May 2007.
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Doster, W. The dynamical transition of proteins, concepts and misconceptions. Eur Biophys J 37, 591–602 (2008). https://doi.org/10.1007/s00249-008-0274-3
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DOI: https://doi.org/10.1007/s00249-008-0274-3