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Biophysical Journal 69: 1440-1446 (1995)
© 1995 the Biophysical Society

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Characterization of Langmuir-Blodgett films of rhodopsin: thermal stability studies.

L Maxia, G Radicchi, I M Pepe and C Nicolini

Institute of Biophysics, Faculty of Medicine, University of Genova, Italy.

ABSTRACT

Two-dimensional close packing of purified bovine rhodopsin, made by the Langmuir-Blodgett technique, was characterized by small angle x-ray scattering and nanogravimetric measurements. The area occupied by a molecule of rhodopsin in the film was approximately 1100 Angstrum2 and the periodicity of the layers resulted in 59 Angstrum. The circular dichroism measurements showed that bleached rhodopsin in Langmuir-Blodgett film had high thermal stability, in fact, reaching a temperature of 150 degrees C without a loss of the secondary structure. Moreover, when the film was made up in the dark, rhodopsin maintained its stability up to at least 200 degrees C and its characteristic absorbance peak at 500 nm up to about 90 degrees C.






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Copyright © 1995 by the Biophysical Society.