Literature Seminar Abstract
Although x-ray crystallography has been the gold standard, nuclear magnetic resonance spectroscopy (NMR) has also been demonstrated as an effective method for protein structure determination. NMR spectroscopy has the ability to view a protein beyond its static structure; it can yield data that gives information about its dynamic behavior as it interacts with other analytes, solutions, or altered conditions. However, NMR spectroscopy remains limited by the slow tumbling rates of macromolecules with molecular masses greater than 30kDa. Slow molecular tumbling rates broaden spectral linewidths, making elucidation of specific cross peaks challenging. To address this problem, the Wand research group combines the encapsulation of large proteins within reverse micelles suspended in a low viscosity fluid to increase tumbling times and minimize the rotational correlation constant that governs the speed of T2 relaxation. Using previously optimized surfactant mixtures, Nucci et al. demonstrate the successful application of this novel technique towards proteins as well as the promising potential to investigate future, more complex macromolecule analytes.
