Conclusions
-
1.
By a special electrochemical method we have determined the parameters of monolayers of proteins adsorbed on a mercury surface: the surface concentration was 0.10–0.13 μg/cm2, the average thickness was 8–10 Å etc. — which agree with the parameters of irreversibly adsorbed proteins at boundaries of other phases. Proteins adsorbed on the mercury surface in the monolayer are found in the denatured, conformationally-flattened state.
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2.
For low degrees of coverage and at the beginning of accumulation of protein on the mercury surface, deep conformational unfolding of the globular proteins occurs down to a thickness of the polypeptide chain, 5–6 Å.
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3.
In the monolayer, the film of flattened protein is found in a compressed state; in this case, part of the segments of the polypeptide chain are displaced into the volume and formation of a secondary structure occurs. Compression and extension of the protein film is accompanied by fast and reversible rearrangement of the chain segments.
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4.
Surface denaturation and irreversible adsorption of proteins are the principal reasons for the strong inhibition of electrochemical reactions of proteins.
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Translated from Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, No. 10, pp. 2282–2290, October, 1982.
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Kuznetsov, B.A., Shumakovich, G.P. Voltammetric study of conformational changes and properties of a protein monolayer adsorbed on a mercury electrode. Russ Chem Bull 31, 2009–2015 (1982). https://doi.org/10.1007/BF00950643
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DOI: https://doi.org/10.1007/BF00950643