In-cell NMR Spectroscopy: From Molecular Sciences to Cell Biology
Chapter 12: Protein Stability and Weak Intracellular Interactions
Published:09 Dec 2019
A. J. Guseman and G. J. Pielak, in In-cell NMR Spectroscopy: From Molecular Sciences to Cell Biology, ed. Y. Ito, V. Dötsch, and M. Shirakawa, The Royal Society of Chemistry, 2019, ch. 12, pp. 188-206.
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The ability of the crowded and complex cytoplasm to influence protein biophysics arises from two properties. The first property is the volume occupied by the constituent macromolecules, which are present at hundreds of grams per liter. The second property comprises the chemical interactions between these molecules. These chemical interactions are the focus of this chapter. Although individually weak, the high concentration of macromolecules in cells allows these contacts to play vital roles in biology. We provide support for the importance of weak interactions and evaluate the evidence that defines them. Our emphasis is on efforts using nuclear magnetic resonance spectroscopy to study disordered and globular proteins both in cells and under biologically relevant in vitro conditions. We also assess the limitations of the systems and approaches and suggest directions that might solve these problems.