Abstract
We present a synchrotron x-ray diffraction study of melting in stacks of two-dimensional crystalline arrays of the membrane protein bacteriorhodopsin. Two distinct regimes have been found as a function of the intermembrane distance d. In the “coupled” regime for d , 250 A the temperature sTmd of the melting transition decreases with increasing d, demonstrating the effect of the repulsive membrane interactions on the intramembrane protein ordering. For d . 250 A a “decoupled” regime is found with higher T p m independent of d. Below T p m a solid-liquid-solid reentrant behavior is observed as d is increased. [S0031-9007(99)08795-5]
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