Bonding in Protein and Polypeptide Monolayers
- 1 August 1970
- journal article
- research article
- Published by Taylor & Francis in Journal of Macromolecular Science: Part A - Chemistry
- Vol. 4 (5) , 1169-1176
- https://doi.org/10.1080/00222337008061011
Abstract
The logarithm of the surface viscosity of protein and polyamino acid monolayers was found to be a linear function of the surface pressure in agreement with the Moore-Eyring theory. The area of the flow unit was similar for all proteins and corresponded to a segment of the molecule of about seven or eight amino acid residues. The free energies of activation for flow at pH 5.5 were fairly constant, falling between 15.6 and 16.6 kcal mole−1 of flow unit. Evidence was obtained for ascribing a large part of the free energy of activation to the breaking of intermolecular keto-imido hydrogen bonds. The interactions of protein monolayers with mercuric ion in the subphase and with lipid incorporated in the monolayer are discussed.Keywords
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