A theoretical model for the covalent assembly of immunoglobulins. Application to the assembly of human immunoglobulin G in vitro.
A simple theoretical model for the formation of interchain disulfide bonds (covalent assembly) in immunoglobulins has been developed. This model successfully simulates the experimentally determined sequence of disulfide bond formation in vitro for human immunoglobulin G1 and G4 (Petersen, J. G. L., and Dorrington, K. J. (1974) J. Biol. Chem. 249, 5633-5641). The model appears to be generally applicable suggesting that the various pathways of covalent assembly observed in vivo and in vitro reflect structural differences between the immunoglobulin classes and subclasses. The rate of assembly, however, is dependent upon environmental factors.
D004220:Disulfides; D006801:Humans; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D008956:Models, Chemical; D009194:Myeloma Proteins; D011487:Protein Conformation
D004220:Disulfides; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D009194:Myeloma Proteins