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Kinetic study into the irreversible thermal denaturation of bacteriorhodopsin

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We report on a differential scanning calorimetry study of native purple membranes under the following solvent conditions: 50 mM carbonate-bicarbonate, 100 mM NaCl, pH 9.5 and 190 mM phosphate, pH 7.5. The calorimetric transitions for bacteriorhodopsin denaturation are highly scanning-rate dependent, which indicates that the thermal denaturation is under kinetic control. This result is confirmed by a spectrophotometric study on the kinetics of the thermal denaturation of this protein. The calorimetric data at pH 9.5 conform to the two-state irreversible model. Comments are made regarding the information obtainable from differential scanning calorimetry studies on bacteriorhodopsin denaturation and the effect of irreversibility on the stability of membrane proteins.

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Correspondence to: J. M. Sanchez-Ruiz

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Galisteo, M.L., Sanchez-Ruiz, J.M. Kinetic study into the irreversible thermal denaturation of bacteriorhodopsin. Eur Biophys J 22, 25–30 (1993). https://doi.org/10.1007/BF00205809

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Key words

  • Bacteriorhodopsin
  • Irreversible thermal denaturation
  • Differential scanning calorimetry