Protein - Metal Ion Interactions

The activity of a wide range of biomolecules is mediated and regulated by metal ion binding. The high-resolution, quantitative structural and functional measurements provided by AnaLight® instruments allow the researcher to understand the structural changes taking place in biomolecules when they bind metal ions. The structural changes taking place during these interactions can be measured simultaneously in terms of molecular dimensions and molecular fold density. Differential metal ion binding can be assessed not only by affinity, but also in terms of the structural changes brought about on binding to the target protein. AnaLight® provides the measurements to connect the changes in biomolecular structure on metal ion binding with the subsequent changes in biological activity and function, at a resolution not previously available in a laboratory-based technique.

Application notes are available as PDF documents that can be either downloaded or viewed online:

• High-Throughput Measurement of Conformational Changes in Prion Protein on Binding a Range of Divalent Metal Cations (364 Kb)
• Measurement of Conformational Change in Prion Protein on Copper Binding (159 Kb)
• Measurement of Conformational Change in HSA on Copper Binding (89 Kb)
• Measurement of Conformational Change in Prion Protein on Zinc Binding (139 Kb)
• Measurement of Conformational Change in Prion Protein on Calcium Binding (134 Kb)
• Measurement of Conformational Change in Prion Protein on Cadmium Binding (138 Kb)
• Measurement of Conformational Change in Transglutaminase on Calcium Ion Binding (272 Kb)

Visit the InfoZone to view or download published papers and conference posters relevant to this application area.

For further information, or application discussions, please contact: applications@farfield-group.com