ABSTRACT
Proteins vary widely in size, shape, and function, yet they all have the common feature of being surface-active macromolecules. This high interfacial activity arises from the amphipathic nature of proteins, which are composed of polar, hydrophobic, and charged residues. When left unchecked, they accumulate at interfaces, reaching surface concentrations far greater than the corresponding bulk concentration. In most applications this is an undesirable property leading to fouling of surfaces and possible denaturation, aggregation, and loss of activity of the proteins.
