ABSTRACT
The adsorption of proteins is like other amphiphilic molecules, strongly influenced by their stability in solution. Changes in the media surrounding the protein, such as pH, ionic strength, heat, and the presence of an interface, will affect the conformational stability-that is, how stable the secondary and tertiary structures are toward these changes. The consequence can be aggregation/precipitation of the protein, although it is important to bear in mind that aggregation/association of proteins can occur without or with only minor conformational changes (cf. Ref. 1). An example of this is the self-association of proteins such as insulin and f3-lactoglobulin.
