title: In-cell NMR of intrinsically disordered proteins in prokaryotic cells.
abstract: In-cell NMR, i.e., the acquisition of heteronuclear multidimensional NMR of biomacromolecules inside living cells, is, to our knowledge, the only method for investigating the three-dimensional structure and dynamics of proteins at atomic detail in the intracellular environment. Since the inception of the method, intrinsically disordered proteins have been regarded as particular targets for in-cell NMR, due to their expected sensitivity to the molecular crowding in the intracellular environment. While both prokaryotic and eukaryotic cells can be used as host cells for in-cell NMR, prokaryotic in-cell NMR, particularly employing commonly used protein overexpression systems in Escherichia coli cells, is the most accessible approach. In this chapter we describe general procedures for obtaining in-cell NMR spectra in E. coli cells.
authors: Department of Chemistry, Tokyo Metropolitan University, Tokyo, Japan. ito-yutaka@tmu.ac.jp
authors: Yutaka
authors: Y
authors: Ito
authors: Tsutomu
authors: T
authors: Mikawa
authors: Brian O
authors: BO
authors: Smith
mesh_terms: D046508:Culture Techniques; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D007553:Isotope Labeling; D019906:Nuclear Magnetic Resonance, Biomolecular; D011387:Prokaryotic Cells / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry
chemical_list: D011994:Recombinant Proteins