Insights into protein function by direct, real-time, structural measurements without tags and the conformation changes associated with ions, pH, other proteins or molecules can be observed at a resolution of less than a tenth of a carbon-carbon bond length. Simultaneous measurements of mass, concentration and density provide a highly correlated perspective of activity, without radioactive or fluorescent tags.
The AnaLight Bio200 has the sensitivity to directly measure proteins changing conformation, as they function. If the function includes mass capture (such as ligand or small molecule binding) there is usually an increase in density, as the binding partner disturbs the site solvation environment. The system has the sensitivity required to detect such density changes. This capability to simultaneously detect binding of small molecules, while measuring conformational changes, provides a highly correlated insight into protein structure, function, and mechanism.
Applications include: protein-protein and molecule-protein interactions; determining specific or non-specific binding of small molecules to proteins; conformational change in proteins as they function; protein aggregation studies; and peptide aggregation studies in neurodegenerative disease research.
Phone: 02 9541 3500
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