Paul R. Edwards

TL;DR: The broader applicability of the RM to studies on molecular interaction studies was demonstrated in an assay for the proteolytic enzyme trypsin and the specific inhibition of enzyme activity by α1-anti-trypsin.

TL;DR: It is suggested that steric hindrance caused by ligate binding to the dextran-coated sensor surface seems the most likely explanation for the observed biphasic association kinetics and that the faster initial phase should be used in oder to determine association constants that can be compared to those in solution.

TL;DR: Initial rate analysis can be successfully applied to analyze experimental binding data generated by an optical biosensor, and the association rate constant obtained is found to be in good agreement with that obtained by the more customary method of nonlinear regression analysis of the entire binding profile.

TL;DR: The past year has seen continuing advances in instrumentation and particularly in novel sensor surfaces, particularly in Novel sensor surfaces of optical biosensors.

TL;DR: It is found that crowding of ligand within this matrix results in a significant reduction in the measured association rate constant, with a corresponding effect in the calculated overall affinity, but measurements at low ligand loadings show association rate constants that are comparable to those measured in solution.