Affinity

• Highest sensitivity
• Bio molecular interactions
• Small molecule binding

An equilibrium measurement and therefore values derived for affinity from either mass binding or conformational change should be identical. This provides a simple and accurate check on the experimental design to ensure there are no measurement artifacts from e.g. non specific binding (which will not induce a conformational change). Similarly, thermodynamic values for ΔG°, ΔH° and ΔS° derived using equilibrium measurements (from the van't Hoff equation) using mass binding or conformational change should be equal providing yet another validation of the experimental design.

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Application notes:

• Affinity studies of Glycoprotein-Lectin Interactions, High Resolution Studies of Lipid Bilayer Formation
  Affinity Studies of Glycoprotein-Lectin Interactions Introduction Dual Polarisation Interferometry (DPI) is an important enabling tool for biochemistry and cell biology.
• Biomolecular Interaction Analysis - Biophysics Applications - Applications
  Biomolecular Interaction Analysis The absolute, multi-parameter measurements provided by Ana Light instruments enable the researcher to explore and understand the structural changes taking place in biomolecules as they function.