NIH Research Festival
The NHLBI Biophysics Core Facility (BCF) provides state of the art equipment and training to assist investigators in studies of macromolecular interactions, dynamics and stability. The BCF currently has resources to study oligomeric state of biomolecular assemblies, perform measurements of affinity, stoichiometry, kinetics and thermodynamics of interactions between proteins, DNA, RNA and their cognate ligands. Biophysical characterization capabilities include measurements of molecular weight, shape, and conformation of biological macromolecules. Oligomeric state of macromolecular assemblies, including their size and shape, can be studied in the BCF using both analytical ultracentrifugation (AUC) and light scattering techniques (SEC-MALS, DLS, AF4, HF5, EFFF, EAF4). The G10 iSCAMS performs precise molecular weight measurements in a single-molecule regime in solution, and the particle tracking technology analyzes particles as large as 2,000 nanometers. Microcalorimetry is the biophysical method of choice for non-invasive, label-free analysis of biomolecular interactions and stability, measuring the heat effect associated with most physical or chemical processes. The BCF has several Isothermal Titration and Differential Scanning Calorimeters (ITC and DSC) that can be used in those studies. Surface Plasmon Resonance and Bio-Layer Interferometry (SPR and BLI) are complimentary methods for studying macromolecular interactions that can also provide information on binding kinetics and the BCF is equipped with the Biacore 3000 and Octet RED96 instruments. Affinities of interactions in biological system can be measured by MicroScale Thermophoresis (MST) method using the Monolith instrument. The BCF users can also take advantage of several optical spectroscopy methods, including steady-state and time resolved fluorescence, fluorescence anisotropy and circular Dichroism (CD).
Scientific Focus Area: Biomedical Engineering and Biophysics
This page was last updated on Friday, March 26, 2021