Publisher Summary The chapter discusses the proteins at interfaces and aims to present protein adsorption and its ramifications, such as the effects of adsorption on conformation and reactivity from a fundamental physicochemical approach Although many proteins are very soluble in water, adsorption leads to stable monolayers that are extremely difficult to desorb Adsorption may be followed at fluid/fluid interfaces by measuring changes in interfacial pressure, potential, or viscosity, using spread monolayers for calibration purposes Before a protein molecule can adsorb and exert its influence at a phase boundary or take part in an interfacial reaction, it must arrive at the interface by a diffusion process At fluid/fluid interfaces, it is established that proteins lose their tertiary structure One of the advantages of the fluid/fluid type interface is that the distribution between adsorbed (trains) and displaced segments (loops) may be quantitatively studied by carrying out measurements with a film balance This approach has been used for spread monolayers of protein The high free energy of adsorption of proteins results in all segments being at the interface at low interfacial pressures The conformational changes that accompany desorption from an interface have direct bearing on the important subject of protein biosynthesis The chapter also discusses the equilibrium aspects of adsorption, reactions at interfaces, and proteins at interfaces in biological systems

Properties and Structure of Protein Monolayers.

Proteins at interfaces.

Rates of evaporation of water through compressed monolayers on water

Publisher Summary There are two methods of affecting spreading of proteins on aqueous surfaces. Hughes and Ridea. Hughes, Fosbinder and Lessig found that solid particles, even of water insoluble proteins, spread very rapidly when carefully placed on the surface. The amount of material spread is determined by a modified Nernst balance. The other method that has several advantages over the solid particle method is to drop on the clean aqueous surface a dilute solution of the protein. In each individual case, the spread areas per unit weight of protein must be demonstrated to be independent of the protein concentration, in the concentration range that is employed. Rideal, Neurath and Gorter find that when a spread protein film is irradiated with ultraviolet light, the film collapses. This collapse is presumably due to fragmentation of the protein molecule by the ultraviolet light with the production of soluble, pressure displaceable material. The nature of the folding of the spread protein as well as the sequence of the amino acid residues in the chain, two problems of great importance to protein chemistry, cannot at the present time be studied by spread film technique.

Properties and Structure of Protein Monolayers.

Citations

Proteins at interfaces.

Rates of evaporation of water through compressed monolayers on water

Spread monolayers of protein.

Surface modification in microsystems and nanosystems

Spread monolayers of proteins

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