Surface Plasmon Resonance

Abstract

Interactions between macromolecules play a central role in most biological processes. Their analysis in vitro can shed light on their role in the intact cell by providing valuable information on specificity, affinity, and structure-function relationships. Significant progress in this respect has come with the advent, in the last few years, of commercially available biosensor technology (1). This has allowed the study of macromolecular interactions in real time, providing a wealth of high-quality binding data that can be used for kinetic analysis, affinity measurements, competition studies, and so on. A major advantage of biosensor analysis is that there is no requirement for labeling one of the interacting components and then separating bound from free molecules—a fact that simplifies experimental procedures and provides more accurate measurements.