Abstract
The forces of interaction between proteins adsorbed onto mica have been measured as a function of the distance of separation between the two mica surfaces in aqueous solutions. The results for three proteins, myelin basic protein, concanavalin A and cytochrome c, are presented together with the results for a model basic protein, poly-( l-lysine). With the exception of cytochrome c at large separations, the forces of interation are due to charges on the protein surfaces and may be fitted closely to theoretical predictions. For cytochrome c, however, no long-range electrical repulsion is observed, indicating that the negatively charged mica surface has been neutralised by the adsorption of the positively charged protein. At short surface separations, an attracton between the protein surfaces was noted. For concanavalin A, a weak attraction was observed in the presence of calcium and manganese ions only. For poly( l-lysine) and cytochrome c the attraction can be explained simply in terms of van der Waals interactions between the proteis. However, for myelin basic protein the observed attraction was an order of magnitude larger than that predicted by van der Waals theory. We believe that this additional attraction may be due to hydrophobic interactions between the adsorbed myelin basic protein molecules.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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