In-cell Structural Biology Through the Integration of Solution NMR Spectroscopy and Computational Science

Abstract

The highly crowded environment of the cytoplasmic spaces of living cells has considerable effects not only on the enzymatic and binding activities, but also on the conformation and dynamics of bio-macromolecules. In-cell NMR spectroscopy is currently the only method capable of analysing the effects of the intracellular crowding on the biophysical properties of bio-macromolecules in real time at atomic resolution. Indeed, in-cell NMR has now been applied to various intracellular events and interesting findings have been reported. Molecular dynamics simulations that consider molecular crowding are also attracting attention as a tool for obtaining a more general picture of the intracellular environment. In this chapter, the results of in-cell NMR studies, particularly in combination with computational science, on the folding stability, 3D structure and dynamics of proteins in cells are discussed.