Abstract
We present a detailed analysis of the picosecond-to-nanosecond motions of green fluorescent protein (GFP) and its hydration water using incoherent and coherent neutron scattering and hydrogen/deuterium contrast. Our results reveal that while much of the dynamics in the hydrated protein are connected to motions of hydration water, there are significant differences in the dynamics of protein and its hydration water. On the picosecond-to-nanosecond timescale, the hydration water exhibits diffusive dynamics, while the protein motions are localized to less than ∼3A. The beta-barrel structure of GFP differs from previously studied globular proteins; which may explain the differences observed in the direct comparison of the atomic displacements (on a timescale of ∼1ns) between GFP and lysozyme. We expand upon this and the recent Biophysical Journal article on this system with a more in depth analysis of the quasielastic spectra and a comparison of the data for GFP to current models for dry and hydrated protein motions. Finally, coherent scattering measurements allow us to comment on the cooperativity of protein and hydration water dynamics.View Large Image | View Hi-Res Image | Download PowerPoint Slide
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