Explanation of anomalous dynamics in the hydration layer

The rotational dynamics on the protein surface is basically shaped by electrostatic interactions alone and the HBs formed by water with the protein surface break the quasi-isotropic nature of the dipolar rotation that is found in the bulk. Also, for the fiilly thermalized protein, a ratio between the characteristic times of the first and the second dipole-dipole correlation function, yff = /r, of about 5 is at variance [Pg.144]

In addition, protein motion reduces the retardation of the water dynamics, because the dimension of the water translational space is increased and at the same time the decay of the orientational correlation is accelerated. In spite of this accelerated dynamics, hydration water diffusion remains anomalous for a thermalized protein. [Pg.144]

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