Abstract
The internal motions of bacteriorhodopsin, the integral membrane protein in purple membranes of Halobacterium halobium, have been studied by neutron scattering as a function of different external conditions. The internal dynamics exhibit a transition above a critical temperature of 230 K from a harmonic to an anharmonic regime, provided the hydration of the membranes is sufficient. We found this onset of large amplitude motions correlated with the appearance of protein function under certain conditions of temperature and relative humidity.
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