BIOC 662 Macromolecular Interactions
Instructor: Ashutosh Tripathy; 962-2362 (Ashutosh_Tripathy@med.unc.edu)
Meeting Dates: (4/1/2024-4/30/2024)
Time: Lectures MWF 11:15AM-12:05PM
Location: GMB 3007; Labs TBA in MacInFac
*Registration limited to 14 students. Cross listed as Chem 735.
Macromolecular Interactions Facility (Mac-In-Fac)
This is a practical course that coordinates lectures with experience in the Macromolecular Interactions Facility. Lectures introduce methods for monitoring interactions of macromolecules with other molecules. Labs offer students hands-on experience with major techniques available in the Facility.
- Measurement of binding using Isothermal Titration Calorimetry (ITC). Setting up an ITC experiment, and analyzing data to obtain stoichiometry (N), dissociation constant (Kd), and other thermodynamic parameters.
- Analytical Ultracentrifugation (AUC): Sedimentation Equilibrium and Sedimentation Velocity. Setting up an AUC experiment to determine molecular weight and oligomeric state of a protein.
- Use of Static and Dynamic Light Scattering to determine molecular weight, root-mean-square radius, hydrodynamic radius, and second virial coefficient of a molecule. Setting up static and dynamic light scattering experiments and analyzing data.
- Use of Surface Plasmon Resonance (SPR) to determine bimolecular interactions. Setting up a SPR experiment, and analyzing data to obtain on and off rates, and binding constants.
- Time permitting – Overview of Fluorescence, Circular Dichroism, Micro-Scale Thermophoresis (MST), nanoDSF, and Octet techniques.