Biomolecular Stability and Structure
Unlike first-generation biosensor technologies, the multi-parameter structural measurements provided by AnaLight® instruments are not dependent on any mass changes taking place in the molecules under investigation. This allows the researcher to explore and understand structural changes in biomolecules brought about by environmental factors such as pH, salt, temperature, solvents and buffers. The correct function of biomolecules is known to be dependent on their structural integrity and stability, and AnaLight® has the unique sensitivity to measure structural changes without mass change. The structural changes taking place are measured simultaneously in terms of molecular dimensions and molecular fold density. AnaLight® provides the measurements to assess changes in biomolecular structure and to explore environmental conditions that either prevent, or cause, these changes 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:Available Downloads
- Quantitative Measurement of Adsorption of pH Dependent Structures Adopted by BSA (130 Kb)
- DPI Characterisation of Antibody Immobilisation (47 Kb)
- Structural and Functional Characterisation of Hydrocortisone - Anti-Hydrocortisone Antibody Interactions (87 Kb)
- Real Time Measurement of Actin Polymerisation by DPI (494 Kb)
- Measuring Early-Stage ß-Amyloid Aggregation using DPI (83 Kb)
- Real Time, High Resolution Studies of Lipid Bilayer Formation (61 Kb)
- The Mechanism of ß-Amyloid Aggregation under Different Surface Conditions (40 Kb)
- Measuring a-Synuclein Aggregation in Wild Type and Mutant Forms using DPI, Orientation and Activity (73 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)
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