Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.

ABSTRACT: We present a detailed analysis of the picosecond-to-nanosecond motions of green fluorescent protein (GFP) and its hydration water using neutron scattering spectroscopy and hydrogen/deuterium contrast. The analysis reveals that hydration water suppresses protein motions at lower temperatures (<~ 200 K), and facilitates protein dynamics at high temperatures. Experimental data demonstrate that the hydration water is harmonic at temperatures <~ 180-190 K and is not affected by the proteins' methyl group rotations. The dynamics of the hydration water exhibits changes at ~ 180-190 K that we ascribe to the glass transition in the hydrated protein. Our results confirm significant differences in the dynamics of protein and its hydration water at high temperatures: on the picosecond-to-nanosecond ti

SUBMITTER: Nickels JD 

PROVIDER: S-EPMC3471459 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature