High-Resolution NMR Studies of Encapsulated Proteins in Liquid Ethane

摘要

Historically,large,aggregation-prone,and membrane proteins have been difficult to examine by modern multinuclear and multidimensional nuclear magnetic resonance (NMR) spectroscopy.A major limitation presented by these kinds of protein systems is that their slow molecular reorientation compromises many aspects of the more powerful solution NMR methods.Several approaches have emerged to deal with the various spectroscopic difficulties arising from slow molecular reorientation.One of these takes the approach of actively seeking to increase the effective rate of molecular reorientation by encapsulating the protein of interest within the protective shell of a reverse micelle and dissolving the resulting particle in a low viscosity fluid.