The antigenic activity of variable (V) and constant (C) domains of mouse myeloma MOPC 21 light (L) chain has been used as a probe of their conformational state. The conformational properties of L-monomers, L-dimers and native IgG1 MOPC 21 protein were investigated by the reaction of inhibition of radioimmunoadsorbtion. Antibodies against the C-domain and different regions of V-domain were used in these experiments. It was shown that V-domain of L-monomers has sharp local conformational disruptions as compared with the native protein, while the conformational state of C-domain remains stable in monomers, dimers and native protein. It was found that the coinformational flexibility of different parts of V-domain of L-monomers is not equal. The antigenic activity of V-domain is partly restored in L-dimers, reaching the conformational state close to that of v-domain in the native protein. The possible interrelation between the conformational properties of V-domains and their functional activity is discussed.
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