Characterization of Langmuir-Blodgett films of rhodopsin: thermal stability studies.
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.
Institute of Biophysics, Faculty of Medicine, University of Genova, Italy.
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Maxia
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Radicchi
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Pepe
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Nicolini
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004355:Drug Stability; D006358:Hot Temperature; D011487:Protein Conformation; D012243:Rhodopsin / Q000737:chemistry* / Q000302:isolation & purification; D012374:Rod Cell Outer Segment; D013816:Thermodynamics; D014961:X-Ray Diffraction / Q000379:methods
D012243:Rhodopsin