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 . In the “coupled” regime for the temperature of the melting transition decreases with increasing , demonstrating the effect of the repulsive membrane interactions on the intramembrane protein ordering. For a “decoupled” regime is found with higher independent of . Below a solid-liquid-solid reentrant behavior is observed as is increased.
- Received 29 September 1998
DOI:https://doi.org/10.1103/PhysRevLett.82.3184
©1999 American Physical Society