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By Fraser Armstrong, Julea Butt, Jacques Breton, Andrew J. Thomson (auth.), Milton J. Allen, Stephen F. Cleary, Arthur E. Sowers, Donald D. Shillady (eds.)

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H. 40 (1987) J. Am. Chern. Soc. 109:3559. Palmer G. (1987) Pure and ADDI. Chern. 59:749. L. D. (1987) J. Am. Chern. Soc. 109:3559. M. (1991) Science 252:1164. R. (1977) Biochern. 16:1377. Smith T. (1980) J. Colloid Interface Sci. 75:51. , and Buse G. (1987) Eur. J. Biochem. 164:295. , and Yu H. (1987) Langmuir 3:932. F. (1991) J. Am. Chern. Soc. 113:1847. L. S. (1988) Ann. Y. Acad. Sci. 550:22. S. (1977) J. BioI. Chern. 252:5498. S. (1988) Proc. Natl. Acad. Sci. USA 85:1354. A. (1984) Biochern.

Mo- 25 lecules quickly desorb from the surface. However, in the case of slow changes of potential, protein molecules have time to reorient into suitable position and remain in adsorbed state. It should be emphasized that the present consideraton of the protein interaction with solid surface is based on many simplifications. Considering the reorientation one have to take into account that protein molecules in the dense and diffuse parts of the double electric layer (DEL) are in high gradients of potential, pH value, ionic strenth, ion concentrations, etc.

The starting temperature for the activation energy measurements. The iodine released into the chamber containing the lipid samples was obtained by diluting a saturated solution of iodine in diethylene glycol. This solvent has a very low vapor pressure and in the absence 55 of iodine does not affect the electrical properties of the lipid films. Dilutions of the saturated solution were used to obtain various "iodine vapor pressures" (Weast, 1983) in the chamber. Numerous control measurements were made to assure that the electrical current observed was due to current through the lipid film with its adsorbed iodine rather than through other components of the experimental system.

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