CALCULATION OF CYS-30 DELTA-PK(A)S AND OXIDIZING POWER FOR DSBA MUTANTS

DsbA possesses a redox active disulphide, with the equilibrium strongl y shifted towards the reduced form as compared to its structural homol ogue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pg, properties for DsbA mutants in this region are available. Elec trostatics calculations show reasonable agreement with the experimenta l data, and support the suggestion that amino acids outside of the CXX C active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.