I have been using the Geysen pin/peptide technique to define B cell
epitopes since 1989 and am sick and tired of arrogant reviewers of papers
and grants pointing out to me that this method is only useful for linear
epitopes which only account for 20% of possible B cell epitopes. Geysen
himself has pointed this out !!
Does anyone know of methods to define conformational epitopes. Of
particular interest to us is - can you get at the region of a protein
(enzyme, toxin) which has a measurable function by inhibiting that
function with monoclonal antibody and then doing what ? Mutating the
protein is of limited value as you can never be sure that your
manipulations do not influence 3-D structure way off from the place you
have messed with
