PREDICTING THE NUMBER OF ELECTROACTIVE DISULFIDE BONDS IN PROTEINS ADSORBED ON MERCURY-ELECTRODES

A method for estimating the number of electroactive disulphide bonds i n proteins was developed based on the assumption that the electroactiv e disulphides are located in the more hydrophobic regions of the prote in. The method used literature values for the relative hydrophobicity of amino acids to arrive at a measure of the relative hydrophobicity o f regions containing disulphide bonds. Threshold values for the calcul ated hydrophobicity were identified which gave a good correlation betw een the number of observed and predicted electroactive disulphide bond s in a variety of proteins.