Phase Behavior and Interactions of the Membrane-Protein Bacteriorhodopsin

I. Koltover, J. O. Raedler, T. Salditt, K. J. Rothschild, and C. R. Safinya
Phys. Rev. Lett. 82, 3184 – Published 12 April 1999
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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 the temperature (Tm) 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 “decoupled” regime is found with higher Tm* independent of d. Below Tm* a solid-liquid-solid reentrant behavior is observed as d is increased.

  • Received 29 September 1998

DOI:https://doi.org/10.1103/PhysRevLett.82.3184

©1999 American Physical Society

Authors & Affiliations

I. Koltover1, J. O. Raedler1, T. Salditt1, K. J. Rothschild2, and C. R. Safinya1

  • 1Materials Department, Physics Department, and Biochemistry and Molecular Biology Program, University of California, Santa Barbara, California 93106
  • 2Department of Physics and Molecular Biophysics Laboratory, Boston University, Boston, Massachusetts 02215

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Vol. 82, Iss. 15 — 12 April 1999

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