Conformational stability of citraconylated ovalbumin.

The lysine residues were modified to varying degrees (50-91%) with citraconic anhydride to determine the extent of conformational change in ovalbumin. Major findings included: 1. Sixteen of the 20 lysine residues are located on the protein surface, while the remaining four are buried. 2. The tertiary structure changed progressively with the degree of modification. 3. However, the secondary structure was disrupted only after one or more of the four buried lysines had been citraconylated. 4. Although the secondary structure was unaltered, the alpha-helix was nevertheless progressively destabilized as the surface 16 lysine residues were modified. This destabilization was due to electrostatic repulsions introduced by the entering citraconyl groups.