Membrane Protein and Lipid Studies
The structural measurements provided by AnaLight® instruments enable the researcher to understand the macrostructures formed by lipids, such as bilayers and liposomes, and to understand how changes in these structures relate to functional events. The affinity and kinetics of lipid - lipid and protein - lipid interactions can be followed through measurement of mass changes with class-leading sensitivity to small mass binders. The structural changes taking place during interactions are measured simultaneously in terms of molecular dimensions and molecular fold density. The structural nature of protein - lipid complexes can be determined through the dimensional and density measurements, revealing information about insertion versus surface binding. The understanding of lipid structures provided by AnaLight® forms a firm basis for the subsequent study of the structure and function of membrane proteins and their interactions in a biomimetic membrane environment.
Application notes are available as PDF documents that can be either downloaded or viewed online:
Available Downloads- Deconstructing Peptide Lipid Interactions with Dual Polarisation Interferometry (DPI) (283 Kb)
- Advantages of UV-ozone cleaned surfaces for the Characterisation Of Lipid Bilayer Membranes-using DPI (180 Kb)
- Working With Lipid Surfaces Using DPI (426 Kb)
- Real Time, High Resolution Studies of Lipid Bilayer Formation (61 Kb)
- High Resolution, Real Time Studies of Protein-Lipid Interactions Using Hemilayer Membrane Mimics (85 Kb)
- The Mechanism of ß-Amyloid Aggregation under Different Surface Conditions (40 Kb)
- Dynamic Measurements of Small Molecule Partitioning into a C18 Membrane Mimic using Dual Polarisation Interferometry (79 Kb)
- Use of DPI to Quantify the Effects of Melittin on Phosphatidyl Choline Liposomes (221 Kb)
- Optimised binding of His-Tagged proteins (128 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
