Biomolecular Interaction Analysis

The absolute, multi-parameter measurements provided by AnaLight® instruments enable the researcher to explore and understand the structural changes taking place in biomolecules as they function. The affinity and kinetics of interactions can be followed through measurement of mass changes with class-leading sensitivity to small mass binders. Additionally, the mass measured by AnaLight® is quantitative, so can also reveal the stoichiometry of interactions. The structural changes taking place during interactions are measured simultaneously in terms of molecular dimensions and molecular fold density, showing dynamic conformational changes and differentiating between specific and non-specific binding events. The structural nature of macromolecular complexes can be determined through the density measurements before and after interaction. AnaLight® provides insights into biomolecular interactions 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:

• Meeting the Challenges of Glycobiology Using DPI (309 Kb)
• Structural and Functional Characterisation of Hydrocortisone - Anti-Hydrocortisone Antibody Interactions (87 Kb)
• High-Throughput Measurement of Conformational Changes in Prion Protein on Binding a Range of Divalent Metal Cations (364 Kb)
• Comparison of Substrate Binding Efficiency of Wild Type and Mutant E.coli KARI (653 Kb)
• Real Time Measurement of Actin Polymerisation by DPI (494 Kb)
• Measuring Early-Stage ß-Amyloid Aggregation using DPI (83 Kb)
• Measurement of Conformational Change in Transglutaminase on Calcium Ion Binding (272 Kb)
• High Resolution, Real Time Studies of Protein-Lipid Interactions Using Hemilayer Membrane Mimics (85 Kb)
• Measurement of Structural Change in Antitrypsin on Small Molecule Binding (206 Kb)
• Measurement of Conformational Change in MAP Kinase on Small Molecule Binding (149 Kb)
• Biotin - Streptavidin Interactions: Measuring Conformational Change and Differentiating between Specific and Non-Specific Binding (188 Kb)
• The Molecular Basis of Action for an Inhibitor of ß-Amyloid Aggregation (73 Kb)
• The Mechanism of ß-Amyloid Aggregation under Different Surface Conditions (40 Kb)
• Affinity studies of Glycoprotein-Lectin Interactions, High Resolution Studies of Lipid Bilayer Formation (132 Kb)
• Measuring a-Synuclein Aggregation in Wild Type and Mutant Forms using DPI, Orientation and Activity (73 Kb)
• Use of DPI to Quantify the Effects of Melittin on Phosphatidyl Choline Liposomes (221 Kb)
• High Resolution Structural Studies of Isoform-Specific Apolipoprotein E Interactions with Tissue Plasminogen Activator (89 Kb)
• Measurement of Conformational Change in P38a/SAPK2a Kinase on Specific Binding of Small Molecules (450 Kb)
• Quantifying the Effects of Dimethyl Sulphoxide (DMSO) on Protein Structure using DPI, Real Time Studies of the Adsorption Behaviour of C12E4 Surfactant (90 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