Sommaire:

Globular proteins are amphiphiles and adsorb to hydrophobic interfaces. Their propensity to change their conformation upon adsorption and to self associate within the interfacial film results in interfacial visco-elasticity and favors foam stabilisation. How is the variability in protein structural and physico-chemical properties reflected in their interfacial behavior? Within the interfacial films, the local protein concentration may reach several hundreds of grams per liter: what can we learn about the interfacial behaviour by studying the structure and osmotic pressure of highly concentrated bulk solutions?

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