Calorimetry instruments are fully automated and require the least amount of sample of any commercially available instruments. Specifically, the facility provides instrumentation and collaborative assistance for:
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Calorimetry instruments are fully automated and require the least amount of sample of any commercially available instruments. Specifically, the facility provides instrumentation and collaborative assistance for:
Full data analysis of the results and assistance with the interpretation of experiments. Assistance with experimental design as it applies to obtaining good calorimetric data.
Differential scanning calorimetry (DSC) is a technique that measures the thermal stability of a macromolecule's tertiary and secondary structure. The raw data obtained in this experiment is a plot of heat capacity difference as a function of temperature, and analysis will yield the macromolecule's Tm as well as the enthalpy of folding.
Isothermal titration calorimetry (ITC) is a technique that measures the heat absorbed or released during a binding event. Integrating the raw data leads to the calculation of the enthalpy of binding. A curve is fit with an appropriate model using the data plot of the enthalpy and ligand-to-macromolecule mole ratio. From this curve the thermodynamic parameters, namely the stoichiometry, dissociation constant, and binding entropy, are obtained.
Quantification provides fast and accurate measure of protein and lipid concentrations, as well as detection of carbohydrates and nucleic acids in samples. Our equipment provides results more quickly and accurately than traditional colorimetric assays.
Multiwavelength analytical ultracentrifugation (MW-AUC) on the Beckman Coulter Optima AUC platform enables high-resolution analysis of complex mixtures by combining sedimentation velocity with full-spectrum UV/Vis detection.
This technique allows for the simultaneous monitoring of multiple species based on both their hydrodynamic and spectral properties, making it particularly powerful for studying interacting systems, co-migrating components, or formulations with overlapping absorbance. MW-AUC provides unique insights into molecular size, shape, stoichiometry, and heterogeneity in native solution conditions, without the need for labeling or immobilization.
Circular dichroism (CD) spectroscopy is a powerful technique for probing the secondary and tertiary structures of proteins, peptides, and other chiral biomolecules in solution.
By measuring the differential absorption of left- and right-circularly polarized light, CD provides insights into the conformational state, folding, stability, and structural changes of macromolecules under varying environmental conditions such as temperature, pH, or ligand binding. It is particularly well-suited for characterizing alpha-helices, beta-sheets, and random coil content, and can be used to monitor folding kinetics or assess the effects of mutations or buffer formulations. CD is a rapid, label-free, and non-destructive method ideal for both routine and advanced structural studies.
The C-Trap® from LUMICKS is a state-of-the-art single-molecule platform that seamlessly integrates optical tweezers, confocal fluorescence, and microfluidics.
This powerful system enables real-time manipulation and visualization of individual biomolecules, allowing researchers to directly measure molecular interactions, conformational changes, and mechanical properties with nanometer precision and piconewton sensitivity. Ideal for studying complex biological processes such as DNA-protein interactions, molecular motors, and nucleic acid mechanics, the C-Trap® provides unparalleled insight into the dynamic behavior of biomolecules at the single-molecule level.