title: In-cell NMR and EPR spectroscopy of biomacromolecules.
abstract: The dream of cell biologists is to be able to watch biological macromolecules perform their duties in the intracellular environment of live cells. Ideally, the observation of both the location and the conformation of these macromolecules with biophysical techniques is desired. The development of many fluorescence techniques, including superresolution fluorescence microscopy, has significantly enhanced our ability to spot proteins and other molecules in the crowded cellular environment. However, the observation of their structure and conformational changes while they attend their business is still very challenging. In principle, NMR and EPR spectroscopy can be used to investigate the conformation and dynamics of biological macromolecules in living cells. The development of in-cell magnetic resonance techniques has demonstrated the feasibility of this approach. Herein we review the different techniques with a focus on liquid-state in-cell NMR spectroscopy, provide an overview of applications, and discuss the challenges that lie ahead.
authors: Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438 Frankfurt (Germany).
authors: Robert
authors: R
authors: Hänsel
authors: Laura M
authors: LM
authors: Luh
authors: Ivan
authors: I
authors: Corbeski
authors: Lukáš
authors: L
authors: Trantirek
authors: Volker
authors: V
authors: Dötsch
mesh_terms: D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D009696:Nucleic Acids / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000378:metabolism
chemical_list: D009696:Nucleic Acids; D011506:Proteins
keywords: G-quadruplexes; in-cell EPR spectroscopy; in-cell NMR spectroscopy; intrinsically disordered  proteins; molecular crowding