A unified model of protein dynamics.
作者： H. Frauenfelder , G. Chen , J. Berendzen , P. W. Fenimore , H. Jansson
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摘要: Protein functions require conformational motions. We show here that the dominant motions are slaved by hydration shell and bulk solvent. The protein contributes structure necessary for function. formulate a model is based on experiments, insights from physics of glass-forming liquids, concepts hierarchically organized energy landscape. To explore effect external fluctuations dynamics, we measure in solvent with broadband dielectric spectroscopy compare them internal measured Mossbauer neutron scattering. result clear. Large-scale to They controlled viscosity, absent solid environment. Internal beta shell, hydration, dehydrated protein. quantitatively predicts rapid increase mean-square displacement above ≈200 K, shows determine temperature- time-dependence passage carbon monoxide through myoglobin, explains nonexponential time dependence relaxation after photodissociation.
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