Application Notes

SPR (SPR) has been demonstrated as a powerful technique for rapid, sensitive, and label-free genetic analysis [1-5]. When the sensor surface is coated with a single sensing (probe) DNA, SPR can be used for both affinity binding studies (i.e., kinetic measurements) and concentration detection of a target DNA. However, the concentration detection levels for SPR and SPR imaging are typically at low nanomolar (nM) [3, 4],

SPR has been demonstrated to be a powerful optical technique for bioaffinity studies at the solid/solution interface. In general, SPR measures the change in refractive index originated from the binding of a solution species with a molecule pre-immobilized onto the SPR sensor chip. The advantages of SPR include its simplicity, high sensitivity, obviation of sample labeling, and amenability for real-time analysis

Flow-injection SPR has been demonstrated as a viable alternative for sensitive detection of heavy metal ions at trace levels [1-4]. The impetus behind using SPR for elemental analysis stems from its high sensitivity, simplicity, compact design (for possible field-based work), and universal detection mechanism (e.g., any elemental species adsorbed onto the SPR sensor can cause a detectable signal). The challenge, however, is to prepare a chemically or

In addition to studies of redox-induced conformational changes of surface-bound proteins (cf. Application Note #102), electrochemical SPR can be used to quantify the amount of metal electrodeposited onto a surface and reorganization of organic thin films upon redox reactions. A BI-SPR 1000 was used to quantify the amount of Cu deposited and stripped during Cu2+ reduction/Cu oxidation in a CuSO4 solution

Both electrochemical and surface plasmon resonance (SPR) techniques measure various processes taking place at or near an electrode surface. Combining the two techniques allows one to obtain new insight into these interfacial processes. One example is redox-induced conformational changes in surface-bound protein molecules. However, most SPR setups are not suitable for monitoring fast kinetics or small thickness variations

Understanding conformational changes in proteins and other biomolecules is important because of their critical roles in many biological functions and processes. These conformational changes are often small and fast, making it difficult to measure and monitor. Surface Plasmon Resonance (SPR) is capable to detect rather small conformational changes in surface bound molecules [1]. However, most SPR setups are not suitable