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Research was conducted to examine the binding between expressed triadin peptides and intact triadin and the ryanodine receptor using affinity chromatography and membrane overlay. The extent of ionic interaction was investigated through the impact of varying the salt concentration of the binding buffer. Results indicate that a particular component of binding is confined to a short segment of triadin despite the occurrence of considerable binding through nonspecific charge attraction.

Triadin has a cytoplasmic region that binds to dihydropyridine receptor (DHPr) which is required for signal transmission during the activation of skeletal muscle. The binding sites of triadin to DHPr(sub 664-799) by use of fusion peptides which encodes rabbit DHPr alpha 1 subunit, have been determined using two monoclonal antibodies with cytoplasmic epitopes to triadin. The binding of radiolabeled DHPr(664-799) to triadin in intact vesicles occurs under reducing and nonreducing conditions.

Studies on the disulfide bond, glycosylation and proteolytic degradation patterns of triadin gives an insight into the structure of the protein. A comparison with other Ca(super 2+) channel proteins reveals a novel role for triadin in muscle activation. The two-dimensional electrophoresis immunoblot of the fragments obtained with the monoclonal antibody, GE4.90 exhibits the presence of many bands. The presence of a beta sheet and an alpha helix are also indicated.