I would be interested to know actually which secondary structure plays (helix, sheet or turns) important role in determining the epitope or commonly form a part of the B-cell epitope?
There is nothing as different secondary structures having different affinities towards B cell receptors, in particular. What ultimately matters is the outermost conformations that are available during the docking of your molecules with the B cell receptor. Hence it is the surface availability of that epitope sequence that matters, not the secondary structure.
For further information, you can refer to this paper:
Article Structural analysis of B-cell epitopes in antibody: Protein complexes