May 15, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its May meeting of 2013 at the Fuji Japanese Sushi & Seafood  Rutgers CABM on Wednesday, May 15, 2013.  [ register ][raw]

Abstract for Talk I:

Biological macromolecules are inherently dynamic and in many cases depend on changes in conformation and flexibility to perform their physiological roles. In order to understand how they function at an atomic level, it is necessary to map the energetic interactions that govern their structures and dynamics. NMR spectroscopy is well suited to addressing this problem, since it can provide detailed information on molecular conformation and internal motions. Many NMR measurements can be interpreted quantitatively in terms of exchange rates or thermodynamic differences between conformational states, such as folded and unfolded or ligand-free and ligand-bound forms. In this regard, biological NMR data are highly complementary to those of biocalorimetry, for example isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC). These methods directly detect the heat absorbed and released during protein binding and folding reactions. In fact, the combination of calorimetric and NMR methods provides a clearer picture of molecular processes than does either technique alone. Microcalorimetry is extremely sensitive to the energetics of conformational transitions and macromolecular interactions. However it can be difficult to relate these measurements to specific changes in molecular structure and flexibility without additional information. Conversely, NMR is sensitive to conformation and dynamics at the level of individual atoms, but thermodynamic information is obtained indirectly. Combining NMR and calorimetric measurements has the potential to improve our understanding of how macromolecular structure, dynamics, energetics and function are related, and to redefine our description of biological systems at the atomic level. I will discuss some recent examples from our lab in which NMR and calorimetry have been applied in concert to study fundamental aspects of protein function including folding, molecular recognition, and allostery.