KINETIC MAPPING OF ANTIBODY BINDING SITES

摘要: ABSTRACT The specificity and affinity exhibited by the binding sites of antibodies is a result interactions particular spatial combination certain residues within site with complementary counterpart groups hapten. dynamic equilibrium between hapten antibody has been shown to involve single step: Ab + Hk12/k21 AbH In order probe dimensions combining determine nature localization attracting forces, correlation structure series systematically varied ligands their specific rates (k12) dissociation (k21) carried out using chemical relaxation T-jump method these rates. homogeneous murine IgA protein 315 which polynitrophenyl derivatives probed over 40 different ligands. results enabled construction proposed model for site; four subsites interaction are observed: (a) subsite, (b) two hydrophobic subsites, (c) an electrostatic (positive) subsitg. overall minimal this 12 × 6A. Another at present being studied that phosphoryl choline HOPC 8. Normally induced, heterogeneous oligoalanine peptides have also investigated kinetic method. Specific were determined haptens lengths eluates population. Using fluorescent probes, covalently attached (oligoalanines or DNP) depth examined. This accomplished measurements circular linear polarized components bound carrying fluorophores.